K. V. Rajagopalan | Scholars@Duke

K. V. Rajagopalan
Professor Emeritus of Biochemistry

Research Abstract

The research in our laboratory deals with the chemistry and biology of enzymes in which the element molybdenum is an essential constituent. Recent studies in the laboratory have led to the discovery and characterization of a novel prosthetic group, called molybdopterin, shown to be present in all Mo-containing enzymes (except nitrogenase) and is intimately involved in the catalytic activity associated with the molybdenum centers of the enzymes. More recently molybdopterin has been shown to be present in tungsten containing enzymes from hyperthermophilic archaea. A human genetic deficiency in which the patients display combined deficiencies of all molybdoenzyme activities and suffer from severe neuropathology leading to childhood death has been characterized as resulting from lesions in the biosynthesis of molybdopterin. Current research is directed at areas such as the pathway of biosynthesis of molybdopterin in bacteria and in humans, structural and chemical aspects of the interaction of molybdopterin with molybdoenzymes, and the use of cloned native and mutant genes of molybdoenzymes in structure-function studies of the Mo ligand field and electron transfer reactions in the enzymes. Many of these studies involve the use of techniques such as UV-Visible, fluorescence, EPR, NMR and laser Raman spectroscopies.

Current Appointments & Affiliations

Professor Emeritus of Biochemistry, Biochemistry, Basic Science Departments 2010

Contact Information

225A Nanaline H Duke, Durham, NC 27708
Box 3711 Med Ctr, Durham, NC 27710
raj@biochem.duke.edu (919) 681-8845

Background
Education, Training, & Certifications
- Ph.D., University of Madras (India) 1957
- M.S., University of Madras (India) 1954
- B.S., University of Madras (India) 1951
Duke Appointment History
- Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 1959 - 2014
- Professor of Biochemistry with Tenure, Biochemistry, Basic Science Departments 1975 - 2009
- Associate Professor of Biochemistry with tenure in the Department of Biochemistry, Biochemistry, Basic Science Departments 1971 - 1975
- Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 1967 - 1971
- Associate, Biochemistry, Basic Science Departments 1966
Research
Selected Grants
- Structure And Function Of Enzymes--Role Of Metals awarded by National Institutes of Health 1977 - 2009
- Structure And Function Of Enzymes--Role Of Metals awarded by National Institutes of Health 1977 - 2008
- Molybdenum and the Molybdenum Cofactor in Health awarded by National Institutes of Health 1990 - 2005
- Structure And Function Of Enzymes-Role Of Metals awarded by National Institutes of Health 1996 - 1999
- Structure And Function Of Enzymes - Role Of Metals awarded by National Institutes of Health 1977 - 1999
- Molybdenum & The Molybdenum Cofactor In Human Health awarded by National Institutes of Health 1995 - 1999
- Molybdenum And The Molybdenum Cofacter In Human Health awarded by National Institutes of Health 1990 - 1999
- Molybdenum Andt He Molybdenum Cofactor In Human Health awarded by National Institutes of Health 1990 - 1999
- Structure And Function Of Enzymens-Role Of Metals awarded by National Institutes of Health 1993 - 1996
- Structure And Function Of Enzymes-Role Of Metals awarded by National Institutes of Health 1992 - 1996
- Structure And Function Of Enzymes Role Of Metals awarded by National Institutes of Health 1977 - 1996
- Molybdenum And The Molybdenum Cofactor In Human Health awarded by National Institutes of Health 1994 - 1995
- Molybdenum And The Molybdenum Cofactor In Human Health awarded by National Institutes of Health 1993 - 1995
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Wilson, Heather L., and K. V. Rajagopalan. “The role of tyrosine 343 in substrate binding and catalysis by human sulfite oxidase.” J Biol Chem 279, no. 15 (April 9, 2004): 15105–13. https://doi.org/10.1074/jbc.M314288200.
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  - Feng, Changjian, Heather L. Wilson, John K. Hurley, James T. Hazzard, Gordon Tollin, K. V. Rajagopalan, and John H. Enemark. “Essential role of conserved arginine 160 in intramolecular electron transfer in human sulfite oxidase.” Biochemistry 42, no. 42 (October 28, 2003): 12235–42. https://doi.org/10.1021/bi0350194.
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  - Leimkuhler, Silke, Andrea Freuer, Jose Angel Santamaria Araujo, K. V. Rajagopalan, and Ralf R. Mendel. “Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency.” J Biol Chem 278, no. 28 (July 11, 2003): 26127–34. https://doi.org/10.1074/jbc.M303092200.
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  - Rudolph, Michael J., Jean L. Johnson, K. V. Rajagopalan, and Caroline Kisker. “The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.” Acta Crystallogr D Biol Crystallogr 59, no. Pt 7 (July 2003): 1183–91. https://doi.org/10.1107/s0907444903009934.
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  - Leimkuhler, Silke, Rachael Hodson, Graham N. George, and K. V. Rajagopalan. “Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans.” J Biol Chem 278, no. 23 (June 6, 2003): 20802–11. https://doi.org/10.1074/jbc.M303091200.
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  - Rudolph, Michael J., Margot M. Wuebbens, Oliver Turque, K. V. Rajagopalan, and Hermann Schindelin. “Structural studies of molybdopterin synthase provide insights into its catalytic mechanism.” J Biol Chem 278, no. 16 (April 18, 2003): 14514–22. https://doi.org/10.1074/jbc.M300449200.
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  - Wuebbens, Margot M., and K. V. Rajagopalan. “Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis.” J Biol Chem 278, no. 16 (April 18, 2003): 14523–32. https://doi.org/10.1074/jbc.M300453200.
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  - Feng, Changjian, Heather L. Wilson, John K. Hurley, James T. Hazzard, Gordon Tollin, K. V. Rajagopalan, and John H. Enemark. “Role of conserved tyrosine 343 in intramolecular electron transfer in human sulfite oxidase.” J Biol Chem 278, no. 5 (January 31, 2003): 2913–20. https://doi.org/10.1074/jbc.M210374200.
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  - Raitsimring, Arnold M., Andrei V. Astashkin, Changjian Feng, John H. Enemark, Kimberly Johnson Nelson, and K. V. Rajagopalan. “Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase.” J Biol Inorg Chem 8, no. 1–2 (January 2003): 95–104. https://doi.org/10.1007/s00775-002-0393-8.
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  - Nichols, Jason, and K. V. Rajagopalan. “Escherichia coli MoeA and MogA. Function in metal incorporation step of molybdenum cofactor biosynthesis.” J Biol Chem 277, no. 28 (July 12, 2002): 24995–0. https://doi.org/10.1074/jbc.M203238200.
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  - Johnson, Jean L., Katharine E. Coyne, Robert M. Garrett, Marie-Therese Zabot, Claude Dorche, Caroline Kisker, and K. V. Rajagopalan. “Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients.” Hum Mutat 20, no. 1 (July 2002): 74. https://doi.org/10.1002/humu.9038.
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  - Astashkin, Andrei V., Arnold M. Raitsimring, Changjian Feng, Jean L. Johnson, K. V. Rajagopalan, and John H. Enemark. “Pulsed EPR studies of nonexchangeable protons near the Mo(V) center of sulfite oxidase: direct detection of the alpha-proton of the coordinated cysteinyl residue and structural implications for the active site.” J Am Chem Soc 124, no. 21 (May 29, 2002): 6109–18. https://doi.org/10.1021/ja0115417.
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  - Johnson, J. L., K. V. Rajagopalan, W. O. Renier, I. Van der Burgt, and W. Ruitenbeek. “Isolated sulfite oxidase deficiency: mutation analysis and DNA-based prenatal diagnosis.” Prenat Diagn 22, no. 5 (May 2002): 433–36. https://doi.org/10.1002/pd.335.
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  - Truglio, James J., Karsten Theis, Silke Leimkühler, Roberto Rappa, K. V. Rajagopalan, and Caroline Kisker. “Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.” Structure 10, no. 1 (January 2002): 115–25. https://doi.org/10.1016/s0969-2126(01)00697-9.
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  - Johnson, J. L., K. E. Coyne, K. V. Rajagopalan, J. L. Van Hove, M. Mackay, J. Pitt, and A. Boneh. “Molybdopterin synthase mutations in a mild case of molybdenum cofactor deficiency.” Am J Med Genet 104, no. 2 (November 22, 2001): 169–73. https://doi.org/10.1002/1096-8628(20011122)104:2<169::aid-ajmg1603>3.0.co;2-8.
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  - Lake, M. W., M. M. Wuebbens, K. V. Rajagopalan, and H. Schindelin. “Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.” Nature 414, no. 6861 (November 15, 2001): 325–29. https://doi.org/10.1038/35104586.
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  - Leimkühler, S., M. M. Wuebbens, and K. V. Rajagopalan. “Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor.” J Biol Chem 276, no. 37 (September 14, 2001): 34695–701. https://doi.org/10.1074/jbc.M102787200.
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  - Leimkühler, S., and K. V. Rajagopalan. “A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli.” J Biol Chem 276, no. 25 (June 22, 2001): 22024–31. https://doi.org/10.1074/jbc.M102072200.
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  - Johnson, K. E., and K. V. Rajagopalan. “An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides.” J Biol Chem 276, no. 16 (April 20, 2001): 13178–85. https://doi.org/10.1074/jbc.M010965200.
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  - Xiang, S., J. Nichols, K. V. Rajagopalan, and H. Schindelin. “The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin.” Structure 9, no. 4 (April 4, 2001): 299–310. https://doi.org/10.1016/s0969-2126(01)00588-3.
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  - Leimkühler, S., and K. V. Rajagopalan. “In vitro incorporation of nascent molybdenum cofactor into human sulfite oxidase.” J Biol Chem 276, no. 3 (January 19, 2001): 1837–44. https://doi.org/10.1074/jbc.M007304200.
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  - Rudolph, M. J., M. M. Wuebbens, K. V. Rajagopalan, and H. Schindelin. “Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation.” Nat Struct Biol 8, no. 1 (January 2001): 42–46. https://doi.org/10.1038/83034.
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  - Schindelin, H., C. Kisker, and K. V. Rajagopalan. “Molybdopterin from molybdenum and tungsten enzymes.” Adv Protein Chem 58 (2001): 47–94. https://doi.org/10.1016/s0065-3233(01)58002-x.
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  - Lake, M. W., C. A. Temple, K. V. Rajagopalan, and H. Schindelin. “The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.” J Biol Chem 275, no. 51 (December 22, 2000): 40211–17. https://doi.org/10.1074/jbc.M007406200.
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  - Temple, C. A., and K. V. Rajagopalan. “Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase.” J Biol Chem 275, no. 51 (December 22, 2000): 40202–10. https://doi.org/10.1074/jbc.M007407200.
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  - Temple, C. A., T. N. Graf, and K. V. Rajagopalan. “Optimization of expression of human sulfite oxidase and its molybdenum domain.” Arch Biochem Biophys 383, no. 2 (November 15, 2000): 281–87. https://doi.org/10.1006/abbi.2000.2089.
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  - Temple, C. A., G. N. George, J. C. Hilton, M. J. George, R. C. Prince, M. J. Barber, and K. V. Rajagopalan. “Structure of the molybdenum site of Rhodobacter sphaeroides biotin sulfoxide reductase.” Biochemistry 39, no. 14 (April 11, 2000): 4046–52. https://doi.org/10.1021/bi9921541.
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  - Garton, S. D., C. A. Temple, I. K. Dhawan, M. J. Barber, K. V. Rajagopalan, and M. K. Johnson. “Resonance Raman characterization of biotin sulfoxide reductase. Comparing oxomolybdenum enzymes in the ME(2)SO reductase family.” J Biol Chem 275, no. 10 (March 10, 2000): 6798–6805. https://doi.org/10.1074/jbc.275.10.6798.
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  - Liu, M. T., M. M. Wuebbens, K. V. Rajagopalan, and H. Schindelin. “Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.” J Biol Chem 275, no. 3 (January 21, 2000): 1814–22. https://doi.org/10.1074/jbc.275.3.1814.
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  - Edwards, M. C., J. L. Johnson, B. Marriage, T. N. Graf, K. E. Coyne, K. V. Rajagopalan, and I. M. MacDonald. “Isolated sulfite oxidase deficiency: review of two cases in one family.” Ophthalmology 106, no. 10 (October 1999): 1957–61. https://doi.org/10.1016/S0161-6420(99)90408-6.
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  - Hilton, J. C., C. A. Temple, and K. V. Rajagopalan. “Re-design of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Enhancement of adenosine N1-oxide reductase activity.” J Biol Chem 274, no. 13 (March 26, 1999): 8428–36. https://doi.org/10.1074/jbc.274.13.8428.
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  - Garrett, R. M., J. L. Johnson, T. N. Graf, A. Feigenbaum, and K. V. Rajagopalan. “Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme.” Proc Natl Acad Sci U S A 95, no. 11 (May 26, 1998): 6394–98. https://doi.org/10.1073/pnas.95.11.6394.
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  - Kisker, C., H. Schindelin, A. Pacheco, W. A. Wehbi, R. M. Garrett, K. V. Rajagopalan, J. H. Enemark, and D. C. Rees. “Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.” Cell 91, no. 7 (December 26, 1997): 973–83. https://doi.org/10.1016/s0092-8674(00)80488-2.
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  - Rajagopalan, K. V. “Biosynthesis and processing of the molybdenum cofactors.” Biochem Soc Trans 25, no. 3 (August 1997): 757–61. https://doi.org/10.1042/bst0250757.
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  - Rupar, C. A., J. Gillett, B. A. Gordon, D. A. Ramsay, J. L. Johnson, R. M. Garrett, K. V. Rajagopalan, J. H. Jung, G. S. Bacheyie, and A. R. Sellers. “Isolated sulfite oxidase deficiency.” Neuropediatrics 27, no. 6 (December 1996): 299–304. https://doi.org/10.1055/s-2007-973798.
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  - Joshi, M. S., J. L. Johnson, and K. V. Rajagopalan. “Molybdenum cofactor biosynthesis in Escherichia coli mod and mog mutants.” J Bacteriol 178, no. 14 (July 1996): 4310–12. https://doi.org/10.1128/jb.178.14.4310-4312.1996.
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  - Schindelin, H., C. Kisker, J. Hilton, K. V. Rajagopalan, and D. C. Rees. “Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.” Science 272, no. 5268 (June 14, 1996): 1615–21. https://doi.org/10.1126/science.272.5268.1615.
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  - Hilton, J. C., and K. V. Rajagopalan. “Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter sphaeroides.” Biochim Biophys Acta 1294, no. 2 (May 23, 1996): 111–14. https://doi.org/10.1016/0167-4838(96)00015-5.
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  - Garrett, R. M., and K. V. Rajagopalan. “Site-directed mutagenesis of recombinant sulfite oxidase: identification of cysteine 207 as a ligand of molybdenum.” J Biol Chem 271, no. 13 (March 29, 1996): 7387–91.
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  - Hilton, J. C., and K. V. Rajagopalan. “Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum.” Arch Biochem Biophys 325, no. 1 (January 1, 1996): 139–43. https://doi.org/10.1006/abbi.1996.0017.
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  - Garrett, R. M., D. B. Bellissimo, and K. V. Rajagopalan. “Molecular cloning of human liver sulfite oxidase.” Biochim Biophys Acta 1262, no. 2–3 (June 9, 1995): 147–49. https://doi.org/10.1016/0167-4781(95)00068-r.
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  - Rothery, R. A., J. L. Grant, J. L. Johnson, K. V. Rajagopalan, and J. H. Weiner. “Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation.” J Bacteriol 177, no. 8 (April 1995): 2057–63. https://doi.org/10.1128/jb.177.8.2057-2063.1995.
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  - Kilpatrick, L., K. V. Rajagopalan, J. Hilton, N. R. Bastian, E. I. Stiefel, R. S. Pilato, and T. G. Spiro. “Resonance Raman spectroscopic characterization of the molybdopterin active site of DMSO reductase.” Biochemistry 34, no. 9 (March 7, 1995): 3032–39. https://doi.org/10.1021/bi00009a034.
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  - Wuebbens, M. M., and K. V. Rajagopalan. “Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies.” J Biol Chem 270, no. 3 (January 20, 1995): 1082–87. https://doi.org/10.1074/jbc.270.3.1082.
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  - Johnson, J. L., and K. V. Rajagopalan. “An HPLC assay for detection of elevated urinary S-sulphocysteine, a metabolic marker of sulphite oxidase deficiency.” J Inherit Metab Dis 18, no. 1 (1995): 40–47. https://doi.org/10.1007/BF00711371.
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  - Mize, C., J. L. Johnson, and K. V. Rajagopalan. “Defective molybdopterin biosynthesis: clinical heterogeneity associated with molybdenum cofactor deficiency.” J Inherit Metab Dis 18, no. 3 (1995): 283–90. https://doi.org/10.1007/BF00710416.
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  - Pintos-Morell, G., M. A. Naranjo, M. Artigas, M. Roge, M. Rodes, M. J. Coll, J. L. Johnson, and K. V. Rajagopalan. “Molybdenum cofactor deficiency associated with Dandy-Walker malformation.” J Inherit Metab Dis 18, no. 1 (1995): 86–87. https://doi.org/10.1007/BF00711384.
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  - Joshi, M. S., and K. V. Rajagopalan. “Specific incorporation of molybdopterin in xanthine dehydrogenase of Pseudomonas aeruginosa.” Arch Biochem Biophys 308, no. 2 (February 1, 1994): 331–34. https://doi.org/10.1006/abbi.1994.1047.
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  - Garrett, R. M., and K. V. Rajagopalan. “Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli.” J Biol Chem 269, no. 1 (January 7, 1994): 272–76.
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  - Pitterle, D. M., J. L. Johnson, and K. V. Rajagopalan. “In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene.” J Biol Chem 268, no. 18 (June 25, 1993): 13506–9.
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  - Pitterle, D. M., and K. V. Rajagopalan. “The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor.” J Biol Chem 268, no. 18 (June 25, 1993): 13499–505.
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  - Wuebbens, M. M., and K. V. Rajagopalan. “Structural characterization of a molybdopterin precursor.” J Biol Chem 268, no. 18 (June 25, 1993): 13493–98.
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  - Johnson, J. L., K. V. Rajagopalan, S. Mukund, and M. W. Adams. “Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea.” J Biol Chem 268, no. 7 (March 5, 1993): 4848–52.
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  - Johnson, J. L., K. V. Rajagopalan, and S. K. Wadman. “Human molybdenum cofactor deficiency.” Adv Exp Med Biol 338 (1993): 373–78. https://doi.org/10.1007/978-1-4615-2960-6_77.
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  - Johnson, J. L., and K. V. Rajagopalan. “Molybdopterin biosynthesis in man. Properties of the converting factor in liver tissue from a molybdenum cofactor deficient patient.” Adv Exp Med Biol 338 (1993): 379–82. https://doi.org/10.1007/978-1-4615-2960-6_78.
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  - Rajagopalan, K. V., J. L. Johnson, M. M. Wuebbens, D. M. Pitterle, J. C. Hilton, T. R. Zurick, and R. M. Garrett. “Chemistry and biology of the molybdenum cofactors.” Adv Exp Med Biol 338 (1993): 355–62. https://doi.org/10.1007/978-1-4615-2960-6_74.
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  - Shanmugam, K. T., V. Stewart, R. P. Gunsalus, D. H. Boxer, J. A. Cole, M. Chippaux, J. A. DeMoss, G. Giordano, E. C. Lin, and K. V. Rajagopalan. “Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Salmonella typhimurium.” Mol Microbiol 6, no. 22 (November 1992): 3452–54. https://doi.org/10.1111/j.1365-2958.1992.tb02215.x.
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  - Rajagopalan, K. V., and J. L. Johnson. “The pterin molybdenum cofactors.” J Biol Chem 267, no. 15 (May 25, 1992): 10199–202.
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  - Bastian, N. R., J. L. Johnson, and K. V. Rajagopalan. “31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.” Biofactors 3, no. 3 (January 1992): 197–200.
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  - Bellissimo, D. B., and K. V. Rajagopalan. “Rat sulfite oxidase antibodies cross-react with two gene family-related proteins: albumin and vitamin D-binding protein.” Arch Biochem Biophys 291, no. 1 (November 15, 1991): 168–75. https://doi.org/10.1016/0003-9861(91)90120-8.
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  - Gardlik, S., and K. V. Rajagopalan. “The mechanisms of inactivation of sulfite oxidase by periodate and arsenite.” The Journal of Biological Chemistry 266, no. 25 (September 1991): 16627–32.
  - Johnson, J. L., L. W. Indermaur, and K. V. Rajagopalan. “Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide.” J Biol Chem 266, no. 19 (July 5, 1991): 12140–45.
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  - Johnson, J. L., M. Chaudhury, and K. V. Rajagopalan. “Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa.” Biofactors 3, no. 2 (June 1991): 103–7.
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  - Gardlik, S., and K. V. Rajagopalan. “Oxidation of molybdopterin in sulfite oxidase by ferricyanide. Effect on electron transfer activities.” J Biol Chem 266, no. 8 (March 15, 1991): 4889–95.
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  - Johnson, J. L., N. R. Bastian, N. L. Schauer, J. G. Ferry, and K. V. Rajagopalan. “Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum.” Fems Microbiol Lett 61, no. 2–3 (January 15, 1991): 213–16. https://doi.org/10.1016/0378-1097(91)90554-n.
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  - Bastian, N. R., C. J. Kay, M. J. Barber, and K. V. Rajagopalan. “Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans.” J Biol Chem 266, no. 1 (January 5, 1991): 45–51.
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  - Johnson, J. L., K. V. Rajagopalan, J. T. Lanman, R. B. Schutgens, A. H. van Gennip, P. Sorensen, and D. A. Applegarth. “Prenatal diagnosis of molybdenum cofactor deficiency by assay of sulphite oxidase activity in chorionic villus samples.” J Inherit Metab Dis 14, no. 6 (1991): 932–37. https://doi.org/10.1007/BF01800477.
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  - Rajagopalan, K. V. “Novel aspects of the biochemistry of the molybdenum cofactor.” Adv Enzymol Relat Areas Mol Biol 64 (1991): 215–90. https://doi.org/10.1002/9780470123102.ch5.
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  - Johnson, J. L., K. V. Rajagopalan, and O. Meyer. “Isolation and characterization of a second molybdopterin dinucleotide: molybdopterin cytosine dinucleotide.” Arch Biochem Biophys 283, no. 2 (December 1990): 542–45. https://doi.org/10.1016/0003-9861(90)90681-n.
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  - Hamm-Alvarez, S., A. Sancar, and K. V. Rajagopalan. “The folate cofactor of Escherichia coli DNA photolyase acts catalytically.” J Biol Chem 265, no. 30 (October 25, 1990): 18656–62.
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  - Gardlik, S., and K. V. Rajagopalan. “The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase.” J Biol Chem 265, no. 22 (August 5, 1990): 13047–54.
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  - Hamm-Alvarez, S. F., A. Sancar, and K. V. Rajagopalan. “The presence and distribution of reduced folates in Escherichia coli dihydrofolate reductase mutants.” J Biol Chem 265, no. 17 (June 15, 1990): 9850–56.
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  - Johnson, J. L., N. R. Bastian, and K. V. Rajagopalan. “Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans.” Proc Natl Acad Sci U S A 87, no. 8 (April 1990): 3190–94. https://doi.org/10.1073/pnas.87.8.3190.
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  - Johnson, J. L., R. E. London, and K. V. Rajagopalan. “Covalently bound phosphate residues in bovine milk xanthine oxidase and in glucose oxidase from Aspergillus niger: a reevaluation.” Proc Natl Acad Sci U S A 86, no. 17 (September 1989): 6493–97. https://doi.org/10.1073/pnas.86.17.6493.
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  - Johnson, J. L., M. M. Wuebbens, and K. V. Rajagopalan. “The structure of a molybdopterin precursor. Characterization of a stable, oxidized derivative.” J Biol Chem 264, no. 23 (August 15, 1989): 13440–47.
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  - Hamm-Alvarez, S., A. Sancar, and K. V. Rajagopalan. “Role of enzyme-bound 5,10-methenyltetrahydropteroylpolyglutamate in catalysis by Escherichia coli DNA photolyase.” J Biol Chem 264, no. 16 (June 5, 1989): 9649–56.
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  - Pitterle, D. M., and K. V. Rajagopalan. “Two proteins encoded at the chlA locus constitute the converting factor of Escherichia coli chlA1.” J Bacteriol 171, no. 6 (June 1989): 3373–78. https://doi.org/10.1128/jb.171.6.3373-3378.1989.
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  - Rajagopalan, K. V. “Molybdopterin--problems and perspectives.” Biofactors 1, no. 4 (December 1988): 273–78.
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  - Johnson, J. L., S. Hamm-Alvarez, G. Payne, G. B. Sancar, K. V. Rajagopalan, and A. Sancar. “Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate.” Proc Natl Acad Sci U S A 85, no. 7 (April 1988): 2046–50. https://doi.org/10.1073/pnas.85.7.2046.
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  - Rajagopalan, K. V. “Molybdenum: an essential trace element in human nutrition.” Annu Rev Nutr 8 (1988): 401–27. https://doi.org/10.1146/annurev.nu.08.070188.002153.
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  - Kramer, S. P., J. L. Johnson, A. A. Ribeiro, D. S. Millington, and K. V. Rajagopalan. “The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.” J Biol Chem 262, no. 34 (December 5, 1987): 16357–63.
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  - Gardlik, S., M. J. Barber, and K. V. Rajagopalan. “A molybdopterin-free form of xanthine oxidase.” Arch Biochem Biophys 259, no. 2 (December 1987): 363–71. https://doi.org/10.1016/0003-9861(87)90502-9.
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  - Rajagopalan, K. V. “Molybdenum--an essential trace element.” Nutr Rev 45, no. 11 (November 1987): 321–28. https://doi.org/10.1111/j.1753-4887.1987.tb00981.x.
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  - Johnson, M. E., and K. V. Rajagopalan. “In vitro system for molybdopterin biosynthesis.” J Bacteriol 169, no. 1 (January 1987): 110–16. https://doi.org/10.1128/jb.169.1.110-116.1987.
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  - Johnson, M. E., and K. V. Rajagopalan. “Involvement of chlA, E, M, and N loci in Escherichia coli molybdopterin biosynthesis.” J Bacteriol 169, no. 1 (January 1987): 117–25. https://doi.org/10.1128/jb.169.1.117-125.1987.
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  - Hageman, R. V., and K. V. Rajagopalan. “Assay and detection of the molybdenum cofactor.” Methods Enzymol 122 (1986): 399–412. https://doi.org/10.1016/0076-6879(86)22200-4.
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  - Rajagopalan, K. V. “Chemistry and biology of the molybdenum cofactor.” Biochem Soc Trans 13, no. 2 (April 1985): 401–3. https://doi.org/10.1042/bst0130401.
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  - Kramer, S., R. V. Hageman, and K. V. Rajagopalan. “In vitro reconstitution of nitrate reductase activity of the Neurospora crassa mutant nit-1: specific incorporation of molybdopterin.” Arch Biochem Biophys 233, no. 2 (September 1984): 821–29. https://doi.org/10.1016/0003-9861(84)90511-3.
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  - Johnson, J. L., B. E. Hainline, K. V. Rajagopalan, and B. H. Arison. “The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.” J Biol Chem 259, no. 9 (May 10, 1984): 5414–22.
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  - Meyer, O., and K. V. Rajagopalan. “Selenite binding to carbon monoxide oxidase from Pseudomonas carboxydovorans. Selenium binds covalently to the protein and activates specifically the CO----methylene blue reaction.” J Biol Chem 259, no. 9 (May 10, 1984): 5612–17.
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  - Wahl, R. C., R. V. Hageman, and K. V. Rajagopalan. “The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor.” Arch Biochem Biophys 230, no. 1 (April 1984): 264–73. https://doi.org/10.1016/0003-9861(84)90107-3.
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  - Meyer, O., and K. V. Rajagopalan. “Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria.” J Bacteriol 157, no. 2 (February 1984): 643–48. https://doi.org/10.1128/jb.157.2.643-648.1984.
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  - Solomonson, L. P., M. J. Barber, W. D. Howard, J. L. Johnson, and K. V. Rajagopalan. “Electron paramagnetic resonance studies on the molybdenum center of assimilatory NADH:nitrate reductase from Chlorella vulgaris.” J Biol Chem 259, no. 2 (January 25, 1984): 849–53.
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  - Wadman, S. K., M. Duran, F. A. Beemer, B. P. Cats, J. L. Johnson, K. V. Rajagopalan, J. M. Saudubray, H. Ogier, C. Charpentier, and R. Berger. “Absence of hepatic molybdenum cofactor: an inborn error of metabolism leading to a combined deficiency of sulphite oxidase and xanthine dehydrogenase.” J Inherit Metab Dis 6 Suppl 1 (1983): 78–83. https://doi.org/10.1007/BF01811328.
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  - Johnson, J. L., and K. V. Rajagopalan. “Structural and metabolic relationship between the molybdenum cofactor and urothione.” Proc Natl Acad Sci U S A 79, no. 22 (November 1982): 6856–60. https://doi.org/10.1073/pnas.79.22.6856.
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  - Barber, M. J., M. P. Coughlan, K. V. Rajagopalan, and L. M. Siegel. “Properties of the prosthetic groups of rabbit liver aldehyde oxidase: a comparison of molybdenum hydroxylase enzymes.” Biochemistry 21, no. 15 (July 20, 1982): 3561–68. https://doi.org/10.1021/bi00258a006.
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  - Rajagopalan, K. V., J. L. Johnson, and B. E. Hainline. “The pterin of the molybdenum cofactor.” Fed Proc 41, no. 9 (July 1982): 2608–12.
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  - Mihara, K., T. Omura, T. Harano, S. Brenner, S. Fleischer, K. V. Rajagopalan, and G. Blobel. “Rat liver L-glutamate dehydrogenase, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and sulfite oxidase are each synthesized as larger precursors by cytoplasmic free polysomes.” J Biol Chem 257, no. 7 (April 10, 1982): 3355–58.
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  - Wahl, R. C., C. K. Warner, V. Finnerty, and K. V. Rajagopalan. “Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases.” The Journal of Biological Chemistry 257, no. 7 (April 1982): 3958–62.
  - Wahl, R. C., and K. V. Rajagopalan. “Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases.” J Biol Chem 257, no. 3 (February 10, 1982): 1354–59.
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  - Speck, S. H., W. H. Koppenol, J. K. Dethmers, N. Osheroff, E. Margoliash, and K. V. Rajagopalan. “Definition of cytochrome c binding domains by chemical modification. Interaction of horse cytochrome c with beef sulfite oxidase and analysis of steady state kinetics.” J Biol Chem 256, no. 14 (July 25, 1981): 7394–7400.
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  - Beemer, F. A., M. Duran, S. K. Wadman, J. L. Johnson, and K. V. Rajagopalan. “Molybdenum metabolism.” Am J Dis Child 134, no. 11 (November 1980): 1097–98. https://doi.org/10.1001/archpedi.1980.02130230075027.
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  - Johnson, J. L., W. R. Waud, K. V. Rajagopalan, M. Duran, F. A. Beemer, and S. K. Wadman. “Inborn errors of molybdenum metabolism: combined deficiencies of sulfite oxidase and xanthine dehydrogenase in a patient lacking the molybdenum cofactor.” Proc Natl Acad Sci U S A 77, no. 6 (June 1980): 3715–19. https://doi.org/10.1073/pnas.77.6.3715.
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  - Barber, M. J., M. P. Coughlan, M. Kanda, and K. V. Rajagopalan. “Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase.” Arch Biochem Biophys 201, no. 2 (May 1980): 468–75. https://doi.org/10.1016/0003-9861(80)90535-4.
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  - Coughlan, M. P., J. L. Johnson, and K. V. Rajagopalan. “Mechanisms of inactivation of molybdoenzymes by cyanide.” The Journal of Biological Chemistry 255, no. 7 (April 1980): 2694–99.
  - Johnson, J. L., B. E. Hainline, and K. V. Rajagopalan. “Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.” J Biol Chem 255, no. 5 (March 10, 1980): 1783–86.
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  - Coughlan, M. P., and K. V. Rajagopalan. “The kinetic mechanism of xanthine dehydrogenase and related enzymes.” Eur J Biochem 105, no. 1 (March 1980): 81–84. https://doi.org/10.1111/j.1432-1033.1980.tb04476.x.
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  - Cramer, S. P., J. L. Johnson, K. V. Rajagopalan, and T. N. Sorrell. “Observation of 17O effects on MoV EPR spectra in sulfite oxidase, xanthine dehydrogenase, and MoO(SC6H5)4-.” Biochem Biophys Res Commun 91, no. 2 (November 28, 1979): 434–39. https://doi.org/10.1016/0006-291x(79)91540-7.
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  - Coughlan, M. P., S. L. Betcher-Lange, and K. V. Rajagopalan. “Isolation of the domain containing the molybdenum, iron-sulfur I, and iron-sulfur II centers of chicken liver xanthine dehydrogenase.” J Biol Chem 254, no. 21 (November 10, 1979): 10694–99.
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  - Amy, N. K., and K. V. Rajagopalan. “Characterization of molybdenum cofactor from Escherichia coli.” J Bacteriol 140, no. 1 (October 1979): 114–24. https://doi.org/10.1128/jb.140.1.114-124.1979.
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  - Betcher-Lange, S. L., M. P. Coughlan, and K. V. Rajagopalan. “Syncatalytic modification of chicken liver xanthine dehydrogenase by hydrogen peroxide. The nature of the reaction.” J Biol Chem 254, no. 18 (September 25, 1979): 8825–29.
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  - Johnson, J. L., and K. V. Rajagopalan. “The oxidation of sulphite in animals systems.” Ciba Found Symp, no. 72 (1979): 119–33. https://doi.org/10.1002/9780470720554.ch8.
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  - Southerland, W. M., D. R. Winge, and K. V. Rajagopalan. “The domains of rat liver sulfite oxidase. Proteolytic separation and characterization.” J Biol Chem 253, no. 24 (December 25, 1978): 8747–52.
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  - Southerland, W. M., and K. V. Rajagopalan. “Domain interactions in oxidized and reduced forms of rat liver sulfite oxidase.” J Biol Chem 253, no. 24 (December 25, 1978): 8753–58.
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  - Winge, D. R., R. Premakumar, and K. V. Rajagopalan. “Studies on the zinc content of Cd-induced thionein.” Arch Biochem Biophys 188, no. 2 (June 1978): 466–75. https://doi.org/10.1016/s0003-9861(78)80031-9.
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  - Winge, D. R., W. M. Southerland, and K. V. Rajagopalan. “Structural studies of the heme domain of sulfite oxidase: CNBr fragments.” Biochemistry 17, no. 10 (May 16, 1978): 1846–53. https://doi.org/10.1021/bi00603a007.
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  - Johnson, J. L., and K. V. Rajagopalan. “The interaction of arsenite with the molybdenum center of chicken liver xanthine dehydrogenase.” Bioinorg Chem 8, no. 5 (1978): 439–44. https://doi.org/10.1016/s0006-3061(00)80278-1.
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  - Shih, V. E., I. F. Abroms, J. L. Johnson, M. Carney, R. Mandell, R. M. Robb, J. P. Cloherty, and K. V. Rajagopalan. “Sulfite oxidase deficiency. Biochemical and clinical investigations of a hereditary metabolic disorder in sulfur metabolism.” N Engl J Med 297, no. 19 (November 10, 1977): 1022–28. https://doi.org/10.1056/NEJM197711102971902.
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  - Johnson, J. L., H. P. Jones, and K. V. Rajagopalan. “In vitro reconstitution of demolybdosulfite oxidase by a molybdenum cofactor from rat liver and other sources.” J Biol Chem 252, no. 14 (July 25, 1977): 4994–5003.
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  - Jones, H. P., J. L. Johnson, and K. V. Rajagopalan. “In vitro reconstitution of demolybdosulfite oxidase by molybdate.” J Biol Chem 252, no. 14 (July 25, 1977): 4988–93.
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  - Beem, K. M., D. C. Richardson, and K. V. Rajagopalan. “Metal sites of copper-zinc superoxide dismutase.” Biochemistry 16, no. 9 (May 3, 1977): 1930–36. https://doi.org/10.1021/bi00628a027.
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  - Drew, R. T., J. L. Johnson, and K. V. Rajagopalan. “Sulfite oxidase deficiency.” Arch Environ Health 32, no. 3 (May 1977): 141–42.
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  - Johnson, J. L., and K. V. Rajagopalan. “Tryptic cleavage of rat liver sulfite oxidase. Isolation and characterization of molybdenum and heme domains.” J Biol Chem 252, no. 6 (March 25, 1977): 2017–25.
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  - Johnson, J. L., and K. V. Rajagopalan. “Electron paramagnetic resonance of the tungsten derivative of rat liver sulfite oxidase.” J Biol Chem 251, no. 18 (September 25, 1976): 5505–11.
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  - Johnson, J. L., and K. V. Rajagopalan. “Human sulfite oxidase deficiency. Characterization of the molecular defect in a multicomponent system.” J Clin Invest 58, no. 3 (September 1976): 551–56. https://doi.org/10.1172/JCI108500.
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  - Johnson, J. L., and K. V. Rajagopalan. “Purification and properties of sulfite oxidase from human liver.” The Journal of Clinical Investigation 58, no. 3 (September 1976): 543–50.
  - Waud, W. R., and K. V. Rajagopalan. “Purification and properties of the NAD+-dependent (type D) and O2-dependent (type O) forms of rat liver xanthine dehydrogenase.” Arch Biochem Biophys 172, no. 2 (February 1976): 354–64. https://doi.org/10.1016/0003-9861(76)90087-4.
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  - Waud, W. R., and K. V. Rajagopalan. “The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O).” Arch Biochem Biophys 172, no. 2 (February 1976): 365–79. https://doi.org/10.1016/0003-9861(76)90088-6.
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  - Rajagopalan, K. V., D. R. Winge, and R. Premakumar. “Chemistry and biology of copper-chelatin.” Adv Exp Med Biol 74 (1976): 565–74. https://doi.org/10.1007/978-1-4684-3270-1_47.
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  - Premakumar, R., D. R. Winge, R. D. Wiley, and K. V. Rajagopalan. “Copper-induced synthesis of copper-chelatin in rat liver.” Arch Biochem Biophys 170, no. 1 (September 1975): 267–77. https://doi.org/10.1016/0003-9861(75)90117-4.
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  - Premakumar, R., D. R. Winge, R. D. Wiley, and K. V. Rajagopalan. “Copper-chelatin: isolation from various eucaryotic sources.” Arch Biochem Biophys 170, no. 1 (September 1975): 278–88. https://doi.org/10.1016/0003-9861(75)90118-6.
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  - Winge, D. R., R. Premakumar, R. D. Wiley, and K. V. Rajagopalan. “Copper-chelatin: purification and properties of a copper-binding protein from rat liver.” Arch Biochem Biophys 170, no. 1 (September 1975): 253–66. https://doi.org/10.1016/0003-9861(75)90116-2.
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  - Winge, D. R., R. Premakumar, and K. V. Rajagopalan. “Metal-induced formation of metallothionein in rat liver.” Arch Biochem Biophys 170, no. 1 (September 1975): 242–52. https://doi.org/10.1016/0003-9861(75)90115-0.
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  - Waud, W. R., F. O. Brady, R. D. Wiley, and K. V. Rajagopalan. “A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure.” Arch Biochem Biophys 169, no. 2 (August 1975): 695–701. https://doi.org/10.1016/0003-9861(75)90214-3.
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  - Johnston, R. B., B. B. Keele, H. P. Misra, J. E. Lehmeyer, L. S. Webb, R. L. Baehner, and K. V. RaJagopalan. “The role of superoxide anion generation in phagocytic bactericidal activity. Studies with normal and chronic granulomatous disease leukocytes.” J Clin Invest 55, no. 6 (June 1975): 1357–72. https://doi.org/10.1172/JCI108055.
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  - Kessler, D. L., and K. V. Rajagopalan. “Hepatic sulfite oxidase. Effect of anions on interaction with cytochrome c.” Biochim Biophys Acta 370, no. 2 (December 29, 1974): 389–98. https://doi.org/10.1016/0005-2744(74)90100-4.
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  - Kessler, D. L., and K. V. Rajagopalan. “Hepatic sulfite oxidase. Identification of the molybdenum center as the site of irreversible inactivation by ferricyanide.” Biochim Biophys Acta 370, no. 2 (December 29, 1974): 399–409. https://doi.org/10.1016/0005-2744(74)90101-6.
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  - Beem, K. M., W. E. Rich, and K. V. Rajagopalan. “Total reconstitution of copper-zinc superoxide dismutase.” J Biol Chem 249, no. 22 (November 25, 1974): 7298–7305.
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  - Cohen, H. J., J. L. Johnson, and K. V. Rajagopalan. “Molecular basis of the biological function of molybdenum. Developmental patterns of sulfite oxidase and xanthine oxidase in the rat.” Arch Biochem Biophys 164, no. 2 (October 1974): 440–46. https://doi.org/10.1016/0003-9861(74)90053-8.
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  - Johnson, J. L., H. J. Cohen, and K. V. Rajagopalan. “Molecular basis of the biological function of molybdenum. Molybdenum-free sulfite oxidase from livers of tungsten-treated rats.” J Biol Chem 249, no. 16 (August 25, 1974): 5046–55.
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  - Johnson, J. L., W. R. Waud, H. J. Cohen, and K. V. Rajagopalan. “Molecular basis of the biological function of molybdenum. Molybdenum-free xanthine oxidase from livers of tungsten-treated rats.” J Biol Chem 249, no. 16 (August 25, 1974): 5056–61.
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  - Johnson, J. L., H. J. Cohen, and K. V. Rajagopalan. “Studies of vanadium toxicity in the rat. Lack of correlation with molybdenum utilization.” Biochem Biophys Res Commun 56, no. 4 (February 27, 1974): 940–46. https://doi.org/10.1016/s0006-291x(74)80279-2.
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  - Johnson, J. L., K. V. Rajagopalan, and H. J. Cohen. “Molecular basis of the biological function of molybdenum. Effect of tungsten on xanthine oxidase and sulfite oxidase in the rat.” J Biol Chem 249, no. 3 (February 10, 1974): 859–66.
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  - Cohen, H. J., R. T. Drew, J. L. Johnson, and K. V. Rajagopalan. “Molecular basis of the biological function of molybdenum: the relationship between sulfite oxidase and the acute toxicity of bisulfite and SO2.” Proc Natl Acad Sci U S A 70, no. 12 (December 1973): 3655–59. https://doi.org/10.1073/pnas.70.12.3655.
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  - Brady, F. O., P. Feigelson, and K. V. Rajagopalan. “Studies of the copper and heme cofactors of pseudomonad L-tryptophan-2,3-dioxygenase by electron paramagnetic resonance spectroscopy.” Arch Biochem Biophys 157, no. 1 (July 1973): 63–72. https://doi.org/10.1016/0003-9861(73)90390-1.
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  - Cohen, H. J., S. Betcher-Lange, D. L. Kessler, and K. V. Rajagopalan. “Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity.” J Biol Chem 247, no. 23 (December 10, 1972): 7759–66.
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  - Winge, D. R., and K. V. Rajagopalan. “Purification and some properties of Cd-binding protein from rat liver.” Arch Biochem Biophys 153, no. 2 (December 1972): 755–62. https://doi.org/10.1016/0003-9861(72)90395-5.
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  - Kessler, D. L., and K. V. Rajagopalan. “Purification and properties of sulfite oxidase from chicken liver. Presence of molybdenum in sulfite oxidase from diverse sources.” J Biol Chem 247, no. 20 (October 25, 1972): 6566–73.
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  - Vance, P. G., B. B. Keele, and K. V. Rajagopalan. “Superoxide dismutase from Streptococcus mutans. Isolation and characterization of two forms of the enzyme.” J Biol Chem 247, no. 15 (August 10, 1972): 4782–86.
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  - Kanda, M., and K. V. Rajagopalan. “Nonequivalence of the flavin adenine dinucleotide moieties of chicken liver xanthine dehydrogenase.” J Biol Chem 247, no. 7 (April 10, 1972): 2177–82.
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  - Weaver, R. F., K. V. Rajagopalan, and P. Handler. “Mechanism of action of a respiratory inhibitor from the gill tissue of the sporulating common mushroom, Agaricus bisporus.” Arch Biochem Biophys 149, no. 2 (April 1972): 541–48. https://doi.org/10.1016/0003-9861(72)90353-0.
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  - Kanda, M., F. O. Brady, K. V. Rajagopalan, and P. Handler. “Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins.” J Biol Chem 247, no. 3 (February 10, 1972): 765–70.
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  - Weaver, R. F., K. V. Rajagopalan, P. Handler, D. Rosenthal, and P. W. Jeffs. “Isolation from the mushroom Agaricus bisporus and chemical synthesis of gamma-L-glutaminyl-4-hydroxybenzene.” J Biol Chem 246, no. 7 (April 10, 1971): 2010–14.
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  - Weaver, R. F., K. V. Rajagopalan, P. Handler, and W. L. Byrne. “Gamma-L-glutaminyl-3,4-benzoquinone. Structural studies and enzymatic synthesis.” J Biol Chem 246, no. 7 (April 10, 1971): 2015–20.
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  - Cohen, H. J., I. Fridovich, and K. V. Rajagopalan. “Hepatic sulfite oxidase. A functional role for molybdenum.” J Biol Chem 246, no. 2 (January 25, 1971): 374–82.
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  - Weaver, R. F., K. V. Rajagopalan, P. Handler, P. Jeffs, W. L. Byrne, and D. Rosenthal. “Isolation of -L-glutaminyl 4-hydroxybenzene and -L-glutaminyl 3,4-benzoquinone: a natural sulfhydryl reagent, from sporulating gill tissue of the mushroom Agaricus bisporus.” Proc Natl Acad Sci U S A 67, no. 2 (October 1970): 1050–56. https://doi.org/10.1073/pnas.67.2.1050.
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  - Rajagopalan, K. V., F. O. Brady, and M. Kanda. “Effect of conformation on the binding of flavins to flavoenzymes.” Vitam Horm 28 (1970): 303–14. https://doi.org/10.1016/s0083-6729(08)60899-7.
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  - Coughlan, M. P., K. V. Rajagopalan, and P. Handler. “The role of molybdenum in xanthine oxidase and related enzymes. Reactivity with cyanide, arsenite, and methanol.” J Biol Chem 244, no. 10 (May 25, 1969): 2658–63.
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  - Rajagopalan, K. V., P. Handler, G. Palmer, and H. Beinert. “Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. II. Kinetic studies by rapid freezing.” J Biol Chem 243, no. 14 (July 25, 1968): 3797–3806.
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  - Rajagopalan, K. V., P. Handler, G. Palmer, and H. Beinert. “Studies of aldehyde oxidase by electron paramagnetic resonance spectroscopy. I. Spectra at equilibrium states.” J Biol Chem 243, no. 14 (July 25, 1968): 3784–96.
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  - Rajagopalan, K. V., and P. Handler. “Purification and properties of chicken liver xanthine dehydrogenase.” J Biol Chem 242, no. 18 (September 25, 1967): 4097–4107.
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  - Smith, S. T., K. V. Rajagopalan, and P. Handler. “Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus.” J Biol Chem 242, no. 18 (September 25, 1967): 4108–17.
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  - RAJAGOPALAN, K. V., and P. HANDLER. “HEPATIC ALDEHYDE OXIDASE. II. DIFFERENTIAL INHIBITION OF ELECTRON TRANSFER TO VARIOUS ELECTRON ACCEPTORS.” J Biol Chem 239 (June 1964): 2022–26.
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  - RAJAGOPALAN, K. V., and P. HANDLER. “HEPATIC ALDEHYDE OXIDASE. 3. THE SUBSTRATE-BINDING SITE.” J Biol Chem 239 (June 1964): 2027–35.
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  - RAJAGOPALAN, K. V., and P. HANDLER. “THE ABSORPTION SPECTRA OF IRON-FLAVOPROTEINS.” J Biol Chem 239 (May 1964): 1509–14.
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  - HANDLER, P., K. V. RAJAGOPALAN, and V. ALEMAN. “STRUCTURE AND FUNCTION OF IRON-FLAVOPROTEINS.” Fed Proc 23 (January 1964): 30–38.
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  - RAJAGOPALAN, K. V., V. ALEMAN, P. HANDLER, W. HEINEN, G. PALMER, and H. BEINERT. “Electron paramagnetic resonance studies of iron reduction and semiquinone formation in metalloflavoproteins.” Biochem Biophys Res Commun 8 (July 3, 1962): 220–26. https://doi.org/10.1016/0006-291x(62)90267-x.
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  - RAJAGOPALAN, K. V., and P. HANDLER. “Oxidation of phenazine methosulfate by hepatic aldehyde oxidase.” Biochem Biophys Res Commun 8 (June 19, 1962): 43–47. https://doi.org/10.1016/0006-291x(62)90232-2.
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  - RAJAGOPALAN, K. V., I. FRIDOVICH, and P. HANDLER. “Hepatic aldehyde oxidase. I. Purification and properties.” J Biol Chem 237 (March 1962): 922–28.
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  - RAJAGOPALAN, K. V., I. FRIDOVICH, and P. HANDLER. “Competitive inhibition of enzyme activity by urea.” J Biol Chem 236 (April 1961): 1059–65.
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  - RAJAGOPALAN, K. V., M. UDAYACHANDER, and P. S. SARMA. “Metabolic effects of isonicotinic acid hydrazid (INH) toxicity in Saccharomyces cerevislae.” Arch Biochem Biophys 87 (April 1960): 184–87. https://doi.org/10.1016/0003-9861(60)90157-0.
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  - RAJAGOPALAN, K. V., T. K. SUNDARAM, and P. S. SARMA. “Metabolism of nicotinamide and nicotinic acid in Corcyra cephalonica St.” Biochem J 74 (February 1960): 355–59. https://doi.org/10.1042/bj0740355.
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  - RAJAGOPALAN, K. V., R. RADHAKRISHNAMURTHY, and P. S. SARMA. “Effect of sulphanilamide on citric acid production by Aspergillus niger.” Nature 184(Suppl 7) (August 8, 1959): 461–62. https://doi.org/10.1038/184461a0.
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  - SUNDARAM, T. K., K. V. RAJAGOPALAN, and P. S. SARMA. “Metabolism of nicotinamide and nicotinic acid in Neurospora crassa.” Biochem J 70, no. 2 (October 1958): 196–201. https://doi.org/10.1042/bj0700196.
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  - RAJAGOPALAN, K. V., T. K. SUNDARAM, and P. S. SARMA. “Biological deamidation of nicotinamide in vertebrates.” Nature 182, no. 4627 (July 5, 1958): 51–52. https://doi.org/10.1038/182051a0.
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  - RAJAGOPALAN, K. V., and P. S. SARMA. “Effect of sulphanilamide on formation of sterols in Saccharomyces cerevisiae and Neurospora crassa.” Biochem J 69, no. 1 (May 1958): 53–56. https://doi.org/10.1042/bj0690053.
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