Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • M.D., Northwestern University
• 

  Duke Appointment History

  • Professor of Biochemistry, Biochemistry, Basic Science Departments 1983 - 2010
  • Dean, Graduate School and Vice Provost, Graduate School, Duke University 1991 - 2006
• Research
• 

  Selected Grants

  • Biological Oxidations In Mitochondria And Microsomes awarded by National Institutes of Health 1988 - 1990
  • Mechanism Of Multielectron Reductases awarded by National Institutes of Health 1987 - 1989
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Crane, B. R., L. M. Siegel, and E. D. Getzoff. “Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.” Biochemistry 36, no. 40 (October 7, 1997): 12120–37. https://doi.org/10.1021/bi971066i.
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    • Crane, B. R., L. M. Siegel, and E. D. Getzoff. “Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange.” Biochemistry 36, no. 40 (October 7, 1997): 12101–19. https://doi.org/10.1021/bi971065q.
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    • Crane, B. R., L. M. Siegel, and E. D. Getzoff. “Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions.” Science 270, no. 5233 (October 6, 1995): 59–67. https://doi.org/10.1126/science.270.5233.59.
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    • Kaufman, J., L. M. Siegel, and L. D. Spicer. “Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands.” Biochemistry 32, no. 34 (August 31, 1993): 8782–91. https://doi.org/10.1021/bi00085a008.
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    • Kaufman, J., L. D. Spicer, and L. M. Siegel. “Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.” Biochemistry 32, no. 11 (March 23, 1993): 2853–67. https://doi.org/10.1021/bi00062a017.
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    • Wu, J. Y., L. M. Siegel, and N. M. Kredich. “High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor.” J Bacteriol 173, no. 1 (January 1991): 325–33. https://doi.org/10.1128/jb.173.1.325-333.1991.
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    • Young, L. J., and L. M. Siegel. “Alkaline low spin form of sulfite reductase hemeprotein subunit.” Biochem Biophys Res Commun 169, no. 1 (May 31, 1990): 39–45. https://doi.org/10.1016/0006-291x(90)91429-v.
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    • Ostrowski, J., M. J. Barber, D. C. Rueger, B. E. Miller, L. M. Siegel, and N. M. Kredich. “Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase.” J Biol Chem 264, no. 27 (September 25, 1989): 15796–808.
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    • Ostrowski, J., J. Y. Wu, D. C. Rueger, B. E. Miller, L. M. Siegel, and N. M. Kredich. “Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.” J Biol Chem 264, no. 26 (September 15, 1989): 15726–37.
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    • Han, S. H., J. F. Madden, L. M. Siegel, and T. G. Spiro. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes.” Biochemistry 28, no. 13 (June 27, 1989): 5477–85. https://doi.org/10.1021/bi00439a024.
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    • Han, S. H., J. F. Madden, R. G. Thompson, S. H. Strauss, L. M. Siegel, and T. G. Spiro. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.” Biochemistry 28, no. 13 (June 27, 1989): 5461–71. https://doi.org/10.1021/bi00439a022.
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    • Madden, J. F., S. H. Han, L. M. Siegel, and T. G. Spiro. “Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.” Biochemistry 28, no. 13 (June 27, 1989): 5471–77. https://doi.org/10.1021/bi00439a023.
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    • HAN, S., J. F. MADDEN, L. M. SIEGEL, and T. G. SPIRO. “NEW INSIGHTS INTO THE SIROHEME-FE4S4 INTERACTION IN SULFITE REDUCTASE FROM RESONANCE RAMAN-SPECTROSCOPY.” Abstracts of Papers of the American Chemical Society 196 (September 25, 1988): 317-INOR.
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    • Young, L. J., and L. M. Siegel. “Superoxidized states of Escherichia coli sulfite reductase heme protein subunit.” Biochemistry 27, no. 16 (August 9, 1988): 5984–90. https://doi.org/10.1021/bi00416a023.
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    • Young, L. J., and L. M. Siegel. “Activated conformers of Escherichia coli sulfite reductase heme protein subunit.” Biochemistry 27, no. 14 (July 12, 1988): 4991–99. https://doi.org/10.1021/bi00414a007.
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    • Young, L. J., and L. M. Siegel. “On the reaction of ferric heme proteins with nitrite and sulfite.” Biochemistry 27, no. 8 (April 19, 1988): 2790–2800. https://doi.org/10.1021/bi00408a020.
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    • Day, E. P., J. Peterson, J. J. Bonvoisin, L. J. Young, J. O. Wilkerson, and L. M. Siegel. “Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S = 1/2 states.” Biochemistry 27, no. 6 (March 22, 1988): 2126–32. https://doi.org/10.1021/bi00406a046.
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    • DAY, E. P., J. BONVOISIN, J. PETERSON, J. WILKERSON, L. J. YOUNG, and L. M. SIEGEL. “THE SULFITE COMPLEX OF SULFITE REDUCTASE - ELECTRON-PARAMAGNETIC-RES SILENT SPIN S= 1/2 STATE.” Abstracts of Papers of the American Chemical Society 194 (August 30, 1987): 134-INOR.
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    • OSTROWSKI, J., E. W. BACK, J. MADDEN, L. M. SIEGEL, and N. M. KREDICH. “COMPARISON OF DEDUCED AMINO-ACID-SEQUENCES OF ALPHA-SUBUNIT AND BETA-SUBUNIT OF SALMONELLA-TYPHIMURIUM NADPH-SULFITE REDUCTASE (SR) WITH THOSE OF SPINACH NITRITE REDUCTASE (NR) AND CYTOCHROME-P-450 OXIDOREDUCTASE (P450R).” Federation Proceedings 46, no. 6 (May 1, 1987): 2231–2231.
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    • Cline, J. F., P. A. Janick, L. M. Siegel, and B. M. Hoffman. “57Fe and 1H electron-nuclear double resonance of three doubly reduced states Escherichia coli sulfite reductase.” Biochemistry 25, no. 16 (August 12, 1986): 4647–54. https://doi.org/10.1021/bi00364a029.
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    • McRee, D. E., D. C. Richardson, J. S. Richardson, and L. M. Siegel. “The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase.” J Biol Chem 261, no. 22 (August 5, 1986): 10277–81.
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    • McRee, D. E., D. C. Richardson, J. S. Richardson, and L. M. Siegel. “The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase.” Journal of Biological Chemistry 261, no. 22 (January 1, 1986): 10277–81.
    • Cline, J. F., P. A. Janick, L. M. Siegel, and B. M. Hoffman. “Electron-nuclear double resonance studies of oxidized Escherichia coli sulfite reductase: 1H, 14N, and 57Fe measurements.” Biochemistry 24, no. 27 (December 31, 1985): 7942–47. https://doi.org/10.1021/bi00348a015.
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    • Coughlan, M. P., R. K. Mehra, M. J. Barber, and L. M. Siegel. “Optical and electron paramagnetic resonance spectroscopic studies on purine hydroxylase II from Aspergillus nidulans.” Arch Biochem Biophys 229, no. 2 (March 1984): 596–603. https://doi.org/10.1016/0003-9861(84)90192-9.
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    • Christner, J. A., E. Münck, T. A. Kent, P. A. Janick, J. C. Salerno, and L. M. Siegel. “Exchange Coupling between Siroheme and [4Fe-4S] Cluster in E. Coli Sulfite Reductase. Mössbauer Studies and Coupling Models for a 2-Electron Reduced Enzyme State and Complexes with Sulfide.” Journal of the American Chemical Society 106, no. 22 (January 1, 1984): 6786–94. https://doi.org/10.1021/ja00334a054.
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    • Barber, M. J., L. M. Siegel, N. L. Schauer, H. D. May, and J. G. Ferry. “Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers.” J Biol Chem 258, no. 18 (September 25, 1983): 10839–45.
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    • Christner, J. A., E. Münck, P. A. Janick, and L. M. Siegel. “Mössbauer evidence for exchange-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex.” J Biol Chem 258, no. 18 (September 25, 1983): 11147–56.
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    • Christner, J. A., P. A. Janick, L. M. Siegel, and E. Münck. “Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster.” J Biol Chem 258, no. 18 (September 25, 1983): 11157–64.
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    • Barber, M. J., G. M. Rosen, L. M. Siegel, and E. J. Rauckman. “Evidence for formation of superoxide and formate radicals in Methanobacterium formicicum.” J Bacteriol 153, no. 3 (March 1983): 1282–86. https://doi.org/10.1128/jb.153.3.1282-1286.1983.
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    • Barber, M. J., and L. M. Siegel. “Electron paramagnetic resonance and potentiometric studies of arsenite interaction with the molybdenum centers of xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: a specific stabilization of the molybdenum(V) oxidation state.” Biochemistry 22, no. 3 (February 1, 1983): 618–24. https://doi.org/10.1021/bi00272a014.
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    • Janick, P. A., D. C. Rueger, R. J. Krueger, M. J. Barber, and L. M. Siegel. “Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite.” Biochemistry 22, no. 2 (January 18, 1983): 396–408. https://doi.org/10.1021/bi00271a025.
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    • Janick, P. A., and L. M. Siegel. “Electron paramagnetic resonance and optical evidence for interaction between siroheme and Fe4S4 prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands.” Biochemistry 22, no. 2 (January 18, 1983): 504–15. https://doi.org/10.1021/bi00271a038.
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    • Münck, Eckard, Jodie A. Christner, Peter A. Janick, and Lewis M. Siegel. “A novel system involving exchange-coupling between a heme and an ironsulfur cluster.” Inorganica Chimica Acta 79 (January 1983): 20–20. https://doi.org/10.1016/s0020-1693(00)95039-4.
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    • WILKERSON, J. O., P. A. JANICK, and L. M. SIEGEL. “SIROHEME-FE4S4 INTERACTION IN SPINACH NITRITE REDUCTASE (NIR).” Federation Proceedings 42, no. 7 (January 1, 1983): 2060–2060.
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    • Wilkerson, J. O., P. A. Janick, and L. M. Siegel. “Electron Paramagnetic Resonance and Optical Spectroscopic Evidence for Interaction between Siroheme and Tetranuclear Iron-Sulfur Center Prosthetic Groups in Spinach Ferredoxin-Nitrite Reductase.” Biochemistry 22, no. 21 (January 1, 1983): 5048–54. https://doi.org/10.1021/bi00290a026.
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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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    • Janick, P. A., and L. M. Siegel. “Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and Fe4S4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit.” Biochemistry 21, no. 15 (July 20, 1982): 3538–47. https://doi.org/10.1021/bi00258a003.
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    • Siegel, L. M., D. C. Rueger, M. J. Barber, R. J. Krueger, N. R. Orme-Johnson, and W. H. Orme-Johnson. “Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.” J Biol Chem 257, no. 11 (June 10, 1982): 6343–50.
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    • Krueger, R. J., and L. M. Siegel. “Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase.” Biochemistry 21, no. 12 (June 8, 1982): 2892–2904. https://doi.org/10.1021/bi00541a014.
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    • Krueger, R. J., and L. M. Siegel. “Evidence for siroheme-Fe4S4 interaction in spinach ferredoxin-sulfite reductase.” Biochemistry 21, no. 12 (June 8, 1982): 2905–9. https://doi.org/10.1021/bi00541a015.
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    • Barber, M. J., J. C. Salerno, and L. M. Siegel. “Magnetic interactions in milk xanthine oxidase.” Biochemistry 21, no. 7 (March 30, 1982): 1648–56. https://doi.org/10.1021/bi00536a027.
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    • Barber, M. J., and L. M. Siegel. “Oxidation-reduction potentials of molybdenum, flavin, and iron-sulfur centers in milk xanthine oxidase: variation with pH.” Biochemistry 21, no. 7 (March 30, 1982): 1638–47. https://doi.org/10.1021/bi00536a026.
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    • Spence, J. T., M. J. Barber, and L. M. Siegel. “Determination of the stoichiometry of electron uptake and the midpoint reduction potentials of milk xanthine oxidase at 25 degrees C by microcoulometry.” Biochemistry 21, no. 7 (March 30, 1982): 1656–61. https://doi.org/10.1021/bi00536a028.
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    • BARBER, M. J., L. M. SIEGEL, N. L. SCHAUER, H. D. MAY, and J. G. FERRY. “METHANOGENESIS - A NOVEL MO CENTER IN METHANOBACTERIUM-FORMICICUM.” Federation Proceedings 41, no. 4 (January 1, 1982): 891–891.
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    • Christner, J. A., E. Münck, P. A. Janick, and L. M. Siegel. “Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups.” J Biol Chem 256, no. 5 (March 10, 1981): 2098–2101.
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    • BARBER, M. J., J. C. SALERNO, and L. M. SIEGEL. “MAGNETIC-INTERACTIONS IN XANTHINE-OXIDASE (XO).” Federation Proceedings 40, no. 6 (January 1, 1981): 1665–1665.
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    • BARBER, M. J., and L. M. SIEGEL. “EFFECT OF PH ON THE REDOX POTENTIALS OF MILK XANTHINE-OXIDASE (XO).” Federation Proceedings 39, no. 6 (January 1, 1980): 1677–1677.
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    • Lancaster, J. R., J. M. Vega, H. Kamin, N. R. Orme-Johnson, W. H. Orme-Johnson, R. J. Krueger, and L. M. Siegel. “Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism.” J Biol Chem 254, no. 4 (February 25, 1979): 1268–72.
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    • Scott, A. I., A. J. Irwin, L. M. Siegel, and J. N. Schoolery. “Sirohydrochlorin. Prosthetic group of a sulfite reductase enzyme and its role in the biosynthesis of vitamin B12.” J Am Chem Soc 100, no. 1 (January 4, 1978): 316–18. https://doi.org/10.1021/ja00469a071.
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    • KRUEGER, R., and L. M. SIEGEL. “SPINACH-FERREDOXIN-SULFITE REDUCTASE (SIR).” Plant Physiology 61, no. 4 (January 1, 1978): 67–67.
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    • Scott, A. I., A. J. Irwin, L. M. Siegel, and J. N. Shoolery. “Sirohydrochlorin.1 Prosthetic Group of Sulfite and Nitrite Reductases and Its Role in the Biosynthesis of Vitamin B12.” Journal of the American Chemical Society 100, no. 25 (January 1, 1978): 7987–94. https://doi.org/10.1021/ja00493a031.
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    • Siegel, L. M., P. S. Davis, and M. J. Murphy. “Incorporation of methionine-derived methyl groups into sirohaem by Escherichia coli.” Biochem J 167, no. 3 (December 1, 1977): 669–74. https://doi.org/10.1042/bj1670669.
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    • Vega, J. M., and R. H. Garrett. “Siroheme: a prosthetic group of the Neurospora crassa assimilatory nitrite reductase.” J Biol Chem 250, no. 20 (October 25, 1975): 7980–89.
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    • Faeder, E. J., P. S. Davis, and L. M. Siegel. “Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleotide prosthetic groups in catalysis.” J Biol Chem 249, no. 5 (March 10, 1974): 1599–1609.
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    • Murphy, M. J., L. M. Siegel, and H. Kamin. “Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme.” J Biol Chem 249, no. 5 (March 10, 1974): 1610–14.
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    • Siegel, L. M., P. S. Davis, and H. Kamin. “Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow.” J Biol Chem 249, no. 5 (March 10, 1974): 1572–86.
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    • Siegel, L. M., and P. S. Davis. “Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components.” J Biol Chem 249, no. 5 (March 10, 1974): 1587–98.
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    • Murphy, M. J., L. M. Siegel, S. R. Tove, and H. Kamin. “Siroheme: a new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases.” Proc Natl Acad Sci U S A 71, no. 3 (March 1974): 612–16. https://doi.org/10.1073/pnas.71.3.612.
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    • Murphy, M. J., and L. M. Siegel. “Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases.” J Biol Chem 248, no. 19 (October 10, 1973): 6911–19.
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    • Murphy, M. J., L. M. Siegel, H. Kamin, D. V. DerVartanian, J. P. Lee, J. LeGall, and H. D. Peck. “An iron tetrahydroporphyrin prosthetic group common to both assimilatory and dissimilatory sulfite reductases.” Biochem Biophys Res Commun 54, no. 1 (September 5, 1973): 82–88. https://doi.org/10.1016/0006-291x(73)90891-7.
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    • Faeder, E. J., and L. M. Siegel. “A rapid micromethod for determination of FMN and FAD in mixtures.” Anal Biochem 53, no. 1 (May 1973): 332–36. https://doi.org/10.1016/0003-2697(73)90442-9.
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    • Siegel, L. M., E. J. Faeder, and H. Kamin. “Flavin interaction in NADPH-sulfite reductase.” Z Naturforsch B 27, no. 9 (September 1972): 1087–89. https://doi.org/10.1515/znb-1972-0929.
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  • Conference Papers

    • Crane, B. R., L. M. Siegel, and E. D. Getzoff. “Crystallographic studies of the multi-electron reductions catalyzed by the siroheme and iron-sulfur cluster-containing enzyme sulfite reductase.” In Acta Crystallographica Section a Foundations of Crystallography, 52:C126–27. International Union of Crystallography (IUCr), 1996. https://doi.org/10.1107/s0108767396094111.
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