Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., University of Texas, Austin 1968
  • B.A., San Diego State University 1964
• 

  Previous Appointments & Affiliations

  • Professor with Tenure, Marine Science and Conservation, Nicholas School of the Environment 1992 - 2011
  • Professor of Cell Biology, Cell Biology, Basic Science Departments 2000 - 2004
  • Professor of Cell Biology, Cell Biology, Basic Science Departments 1994 - 1999
  • Professor, Cell Biology, Basic Science Departments 1993 - 1994
  • Professor with Tenure, Cell Biology, Basic Science Departments 1990 - 1991
  • Associate Professor, Cell Biology, Basic Science Departments 1988 - 1990
  • Associate Professor, Psychology & Neuroscience, Trinity College of Arts & Sciences 1984 - 1988
  • Assistant Medical Research Professor, Biochemistry, Basic Science Departments 1975 - 1984
• Expertise
• 

  Global Scholarship

  • Research

    • North Carolina (State or Province) 
    • United States of America (Country) 
• Research
• 

  Selected Grants

  • Supplement to NSF K-12 Program awarded by  National Science Foundation 2004 - 2005
  • NSF Graduate Teaching Fellows Program of the Duke University Marine Laboratory awarded by  National Science Foundation 2002 - 2005
  • Molecular Controls of Hemoglobin Function awarded by National Institutes of Health 1996 - 2002
  • Marine/Freshwater Biomedical Center awarded by National Institute of Environmental Health Science 1999 - 2002
  • Molecular Controls of Hemoglobin Function awarded by National Institutes of Health 1996 - 2001
  • Molecular Controls of Hemoglobin Function awarded by National Institutes of Health 1996 - 2001
  • Molecular Controls of Hemoglobin Function awarded by National Institutes of Health 1996 - 2001
  • Marine/Freshwater Biomedical Center awarded by National Institutes of Health 2000 - 2001
  • Marine/Freshwater Biomedical Center awarded by National Institutes of Health 1978 - 2001
  • Marine/Freshwater Biomedical Center Grant awarded by National Institute of Environmental Health Science 1978 - 2001
  • (98-0102) Confocal Scanning Microscope and GFP-Fluorescence System awarded by National Institutes of Health 1998 - 1999
  • Unique Marine/Freshwater Models for Environmental Health Research awarded by National Institute of Environmental Health Science 1998 - 1999
  • Marine Freshwater Biomedical Center Grant awarded by National Institute of Environmental Health Science 1978 - 1996
  • Marine/Freshwater Biomedical Center Grant awarded by National Institute of Environmental Health Science 1978 - 1996
  • Pollutant Interactions With Red Cells awarded by National Institutes of Health 1990 - 1992
  • Advanced Research Training In Marine Molecular Biology And awarded by Office of Naval Research 1990 - 1992
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Bonaventura, Celia, Robert Henkens, Abdu I. Alayash, Sambuddha Banerjee, and Alvin L. Crumbliss. “Molecular controls of the oxygenation and redox reactions of hemoglobin.” Antioxidants & Redox Signaling 18, no. 17 (June 2013): 2298–2313. https://doi.org/10.1089/ars.2012.4947.
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    • Banerjee, Sambuddha, Yiping Jia, Claire J Parker Siburt, Bindu Abraham, Francine Wood, Celia Bonaventura, Robert Henkens, Alvin L. Crumbliss, and Abdu I. Alayash. “Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions.” Free Radical Biology & Medicine 53, no. 6 (September 2012): 1317–26. https://doi.org/10.1016/j.freeradbiomed.2012.07.023.
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    • Bonaventura, Celia, Robert Henkens, Joel Friedman, Claire J Parker Siburt, Daniel Kraiter, and Alvin L. Crumbliss. “Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins.” Biochimica Et Biophysica Acta 1814, no. 10 (October 2011): 1261–68. https://doi.org/10.1016/j.bbapap.2011.06.012.
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    • Bonaventura, Celia, Robert Henkens, Walleska De Jesus-Bonilla, Juan Lopez-Garriga, Yiping Jia, Abdu I. Alayash, Claire J Parker Siburt, and Alvin L. Crumbliss. “Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite.” Biochimica Et Biophysica Acta 1804, no. 10 (October 2010): 1988–95. https://doi.org/10.1016/j.bbapap.2010.06.016.
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    • Bonaventura, C. J., R. Henkens, C. Siburt, A. I. Alayash, and A. Crumbliss. “Extreme Differences in Lucina Hemoglobins in their Interactions wtih Nitrite.” Biochemica Biophysica Acta, March 2010.
    • Rittschoff, D., C. J. Bonaventura, and C. Van Dover. “Iron in the Oceans (Approximate title).” Reference Unavailable at This Time (Traveling), July 2008.
    • Rittschof, Dan, Celia Bonaventura, Jonathan J. Wilker, and C. L. Van Dover. “Oxidative iron species and ocean challenges: a perspective.” Biofouling 24, no. 3 (January 2008): 173–75. https://doi.org/10.1080/08927010801958952.
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    • Remington, Nicole, Robert D. Stevens, Randall S. Wells, Aleta Holn, Suraj Dhungana, Celine H. Taboy, Alvin L. Crumbliss, Robert Henkens, and Celia Bonaventura. “Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins.” Gene 398, no. 1–2 (August 15, 2007): 123–31. https://doi.org/10.1016/j.gene.2007.02.050.
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    • Bonaventura, Celia, Robert Henkens, Abdu I. Alayash, and Alvin L. Crumbliss. “Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobins.” Iubmb Life 59, no. 8–9 (August 2007): 498–505. https://doi.org/10.1080/15216540601188546.
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    • Bonaventura, Celia, Gerald Godette, Robert Stevens, Michael Brenowitz, and Robert Henkens. “Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin system.” J Biol Chem 280, no. 49 (December 9, 2005): 40509–14. https://doi.org/10.1074/jbc.M505353200.
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    • Peterson, E., R. Shinder, L. Juczszak, I. Khan, J. Wang, B. Manjula, S. Acharya, C. Bonaventura, and J. Friedman. “-Specific Effector Interactions within the Central Cavity of Hb A0 in Solution and in Porous Sol-gels: Evidence for Long Range Communication Pathways (Accepted).” Biochemistry, 2005.
    • Bonaventura, Celia, Angela Fago, Robert Henkens, and Alvin L. Crumbliss. “Critical redox and allosteric aspects of nitric oxide interactions with hemoglobin.” Antioxidants & Redox Signaling 6, no. 6 (December 2004): 979–91. https://doi.org/10.1089/ars.2004.6.979.
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    • Bonaventura, C., A. L. Crumbliss, and R. E. Weber. “New insights into the proton-dependent oxygen affinity of Root effect haemoglobins.” Acta Physiologica Scandinavica 182, no. 3 (November 2004): 245–58. https://doi.org/10.1111/j.1365-201x.2004.01359.x.
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    • Peterson, Eric S., Roman Shinder, Imran Khan, Laura Juczszak, Jiaqian Wang, Belur Manjula, Seetharama A. Acharya, Celia Bonaventura, and Joel M. Friedman. “Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways.” Biochemistry 43, no. 16 (April 2004): 4832–43. https://doi.org/10.1021/bi035481o.
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    • Bonaventura, C., A. Fago, R. Henkens, and A. Crumbliss. “Forum Review: Critical Redox and Allosteric Aspects of Nitric Oxide Interactions with Hemoglobin.” Antioxidants and Redox Signaling 6, no. 6 (2004): 979–91.
    • Fago, Angela, Alvin L. Crumbliss, Jim Peterson, Linda L. Pearce, and Celia Bonaventura. “The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry.” Proceedings of the National Academy of Sciences of the United States of America 100, no. 21 (October 2003): 12087–92. https://doi.org/10.1073/pnas.2032603100.
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    • Christensen, A. B., J. M. Colacino, and C. Bonaventura. “Functional and biochemical properties of the hemoglobins of the burrowing brittle star Hemipholis elongata say (Echinodermata, Ophiuroidea).” Biological Bulletin 205, no. 1 (2003): 54–65.
    • Gladwin, Mark T., Xunde Wang, Christopher D. Reiter, Benjamin K. Yang, Esther X. Vivas, Celia Bonaventura, and Alan N. Schechter. “S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment and lacks O2/NO-linked allosteric function.” The Journal of Biological Chemistry 277, no. 31 (August 2002): 27818–28. https://doi.org/10.1074/jbc.m203236200.
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    • Bonaventura, Celia, Gerald Godette, Giulia Ferruzzi, Shirley Tesh, Robert D. Stevens, and Robert Henkens. “Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease.” Biophys Chem 98, no. 1–2 (July 10, 2002): 165–81. https://doi.org/10.1016/s0301-4622(02)00092-3.
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    • Bonaventura, Celia, Celine H. Taboy, Philip S. Low, Robert D. Stevens, Celine Lafon, and Alvin L. Crumbliss. “Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells.” J Biol Chem 277, no. 17 (April 26, 2002): 14557–63. https://doi.org/10.1074/jbc.M107658200.
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    • Chen, Q., C. Bonaventura, R. L. Nagel, and R. E. Hirsch. “Distinct domain responses of R-state human hemoglobins A, C, and S to anions.” Blood Cells, Molecules & Diseases 29, no. 1 (2002): 119–32.
    • Juszczak, L. J., B. Manjula, C. Bonaventura, S. A. Acharya, and J. M. Friedman. “UV resonance raman study of β93-modified hemoglobin A: Chemical modifier-specific effects and added influences of attached poly(ethylene glycol) chains.” Biochemistry 41, no. 1 (2002): 376–85. https://doi.org/10.1021/bi011212r.
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    • Taboy, Céline H., Celia Bonaventura, and Alvin L. Crumbliss. “Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry.” Methods in Enzymology 353 (January 2002): 187–209. https://doi.org/10.1016/s0076-6879(02)53048-2.
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    • Khan, I., D. Dantsker, U. Samuni, A. J. Friedman, C. Bonaventura, B. Manjula, S. A. Acharya, and J. M. Friedman. “β93 modified hemoglobin: Kinetic and conformational consequences.” Biochemistry 40, no. 25 (2001): 7581–92.
    • Taboy, C. H., K. M. Faulkner, D. Kraiter, C. Bonaventura, and A. L. Crumbliss. “Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin.” The Journal of Biological Chemistry 275, no. 50 (December 2000): 39048–54. https://doi.org/10.1074/jbc.m004547200.
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    • Bonaventura, C., G. Ferruzzi, S. Tesh, and R. D. Stevens. “Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobin.” J Biol Chem 274, no. 35 (August 27, 1999): 24742–48. https://doi.org/10.1074/jbc.274.35.24742.
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    • Bonaventura, C., G. Godette, S. Tesh, D. E. Holm, J. Bonaventura, A. L. Crumbliss, L. L. Pearce, and J. Peterson. “Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide.” The Journal of Biological Chemistry 274, no. 9 (February 1999): 5499–5507. https://doi.org/10.1074/jbc.274.9.5499.
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    • Taboy, C. H., C. Bonaventura, and A. L. Crumbliss. “Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots.” Bioelectrochemistry and Bioenergetics (Lausanne, Switzerland) 48, no. 1 (February 1999): 79–86. https://doi.org/10.1016/s0302-4598(98)00236-0.
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    • Bonaventura, C. “NIEHS Workshop: Unique Marine/Freshwater Models for Environmental Health Research, Research Triangle Park, North Carolina, 20-21 April 1998.” Environmental Health Perspectives 107, no. 1 (1999): 89–92.
    • Topham, R., S. Tesh, A. Westcott, G. Cole, D. Mercatante, G. Kaufman, and C. Bonaventura. “Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins.” Archives of Biochemistry and Biophysics 369, no. 2 (1999): 261–66. https://doi.org/10.1006/abbi.1999.1367.
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    • Bonaventura, C., S. Tesh, K. M. Faulkner, D. Kraiter, and A. L. Crumbliss. “Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg.” Biochemistry 37, no. 2 (January 1998): 496–506. https://doi.org/10.1021/bi971574s.
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    • Topham, R., S. Tesh, G. Cole, D. Mercatante, A. Westcott, and C. Bonaventura. “Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants. A chemical probe for the study of structure- function relationships in the hemocyanins.” Archives of Biochemistry and Biophysics 352, no. 1 (1998): 103–13. https://doi.org/10.1006/abbi.1998.0574.
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    • Hahn, J. S., R. D. Braun, M. W. Dewhirst, S. Shan, S. A. Snyder, J. M. Taube, E. T. Ong, et al. “Stroma-free human hemoglobin A decreases R3230Ac rat mammary adenocarcinoma blood flow and oxygen partial pressure.” Radiat Res 147, no. 2 (February 1997): 185–94.
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    • Bonaventura, C., and F. M. Johnson. “Healthy environments for healthy people: Bioremediation today and tomorrow.” Environmental Health Perspectives 105, no. SUPPL. 1 (1997): 5–20.
    • Jia, L., C. Bonaventura, J. Bonaventura, and J. S. Stamler. “S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control.” Pneumologie 50, no. 8 (December 1, 1996): 571.
    • Holm, D. E., G. Godette, C. Bonaventura, J. Bonaventura, M. D. Boatright, L. L. Pearce, and J. Peterson. “A carbon monoxide irreducible form of cytochrome c oxidase and other unusual properties of the "monomeric" shark enzyme.” Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 114, no. 4 (August 1996): 345–52. https://doi.org/10.1016/0305-0491(96)00031-4.
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    • Jia, L., C. Bonaventura, J. Bonaventura, and J. S. Stamler. “S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control.” Nature 380, no. 6571 (March 1996): 221–26. https://doi.org/10.1038/380221a0.
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    • Mylvaganam, S. E., C. Bonaventura, J. Bonaventura, and E. D. Getzoff. “Structural basis for the root effect in haemoglobin.” Nature Structural Biology 3, no. 3 (March 1996): 275–83. https://doi.org/10.1038/nsb0396-275.
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    • Swerdlow, R. D., R. F. Ebert, P. Lee, C. Bonaventura, and K. I. Miller. “Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers.” Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 113, no. 3 (March 1996): 537–48. https://doi.org/10.1016/0305-0491(95)02091-8.
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    • Hazes, B., K. A. Magnus, K. H. Kalk, C. Bonaventura, and W. G. J. Hol. “Nitrate binding to limulus polyphemus subunit type II hemocyanin and its functional implications.” Journal of Molecular Biology 262, no. 4 (1996): 532–42. https://doi.org/10.1006/jmbi.1996.0533.
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    • Holm, D. E., G. Godette, J. Bonaventura, C. Bonaventura, and J. Peterson. “The site of the redox-linked proton pump in eukaryotic cytochrome c oxidases.” Febs Letters 370, no. 1–2 (August 1995): 53–58. https://doi.org/10.1016/0014-5793(95)00791-7.
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    • Faulkner, K. M., C. Bonaventura, and A. L. Crumbliss. “A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins.” The Journal of Biological Chemistry 270, no. 23 (June 1995): 13604–12. https://doi.org/10.1074/jbc.270.23.13604.
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    • Bonilla, G. O., A. Focesi Júnior, C. Bonaventura, J. Bonaventura, and R. E. Cashon. “Functional properties of the hemoglobin from the South American snake Mastigodryas bifossatus.” Comparative Biochemistry and Physiology. Part A, Physiology 109, no. 4 (December 1994): 1085–95. https://doi.org/10.1016/0300-9629(94)90258-5.
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    • Bonaventura, C., J. Bonaventura, R. Stevens, and D. Millington. “Acrylamide in polyacrylamide gels can modify proteins during electrophoresis.” Anal Biochem 222, no. 1 (October 1994): 44–48. https://doi.org/10.1006/abio.1994.1451.
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    • Magnus, K. A., B. Hazes, H. Ton-That, C. Bonaventura, J. Bonaventura, and W. G. Hol. “Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.” Proteins 19, no. 4 (August 1994): 302–9. https://doi.org/10.1002/prot.340190405.
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    • Bonaventura, C., M. Arumugam, R. Cashon, J. Bonaventura, and W. F. Moo-Penn. “Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (beta 139 Asn-->Lys) that can modulate cooperativity as well as oxygen affinity.” Journal of Molecular Biology 239, no. 4 (June 1994): 561–68. https://doi.org/10.1006/jmbi.1994.1395.
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    • Stevens, R. D., J. Bonaventura, C. Bonaventura, T. R. Fennel, and D. S. Millington. “Application of electrospray ionization mass spectrometry for analysis of haemoglobin adducts with acrylonitrile.” Biochem Soc Trans 22, no. 2 (May 1994): 543–47. https://doi.org/10.1042/bst0220543.
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    • Faulkner, K. M., C. Bonaventura, and A. L. Crumbliss. “A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins.” Inorganica Chimica Acta 226, no. 1–2 (January 1, 1994): 187–94. https://doi.org/10.1016/0020-1693(94)04086-9.
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    • Alayash, A. I., J. C. Fratantoni, C. Bonaventura, J. Bonaventura, and R. E. Cashon. “Nitric oxide binding to human ferrihemoglobins cross-linked between either alpha or beta subunits.” Archives of Biochemistry and Biophysics 303, no. 2 (June 1993): 332–38. https://doi.org/10.1006/abbi.1993.1292.
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    • Hazes, B., K. A. Magnus, C. Bonaventura, J. Bonaventura, Z. Dauter, K. H. Kalk, and W. G. Hol. “Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.” Protein Science : A Publication of the Protein Society 2, no. 4 (April 1993): 597–619. https://doi.org/10.1002/pro.5560020411.
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    • Alayash, A. I., J. C. Fratantoni, C. Bonaventura, J. Bonaventura, and E. Bucci. “Consequences of chemical modifications on the free radical reactions of human hemoglobin.” Archives of Biochemistry and Biophysics 298, no. 1 (October 1992): 114–20. https://doi.org/10.1016/0003-9861(92)90101-2.
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    • Alayash, A. I., B. A. Ryan, J. C. Fratantoni, J. Bonaventura, and C. Bonaventura. “Hemoglobin-based oxygen carriers (HBOCs): structural alterations that affect free radical generation.” Biomaterials, Artificial Cells, and Immobilization Biotechnology : Official Journal of the International Society for Artificial Cells and Immobilization Biotechnology 20, no. 2–4 (January 1992): 277–81. https://doi.org/10.3109/10731199209119643.
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    • Bonaventura, C., R. Cashon, J. M. Colacino, and R. H. Hilderman. “Alteration of hemoglobin function by diadenosine 5',5'''-P¹,P⁴- tetraphosphate and other alarmones.” Journal of Biological Chemistry 267, no. 7 (1992): 4652–57.
    • Alayash, A. I., B. A. Brockner, J. C. Fratantoni, C. Bonaventura, and J. Bonaventura. “Hemoglobin-based oxygen carriers. Structural alterations that affect free radical formation.” Biomaterials, Artificial Cells, and Immobilization Biotechnology 19, no. 2 (December 1, 1991): 347.
    • Bonaventura, C., R. Cashon, J. Bonaventura, M. Perutz, G. Fermi, and D. T. Shih. “Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66----Thr) and its isolated beta chains.” The Journal of Biological Chemistry 266, no. 34 (December 1991): 23033–40. https://doi.org/10.1016/s0021-9258(18)54459-8.
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    • Boffi, A., C. Bonaventura, J. Bonaventura, R. Cashon, and E. Chiancone. “Oxidized dimeric Scapharca inaequivalvis. Co-driven perturbation of the redox equilibrium.” The Journal of Biological Chemistry 266, no. 27 (September 1991): 17898–903. https://doi.org/10.1016/s0021-9258(18)55212-1.
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    • Ogo, S., A. Focesi, R. Cashon, J. Bonaventura, and C. Bonaventura. “Interactions of nicotinamide adenine dinucleotides with varied states and forms of hemoglobin.” The Journal of Biological Chemistry 264, no. 19 (July 1989): 11302–6. https://doi.org/10.1016/s0021-9258(18)60464-8.
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    • Topham, R., B. Cooper, S. Tesh, G. Godette, C. Bonaventura, and J. Bonaventura. “Isolation, purification and characterization of an iron-binding protein from the horseshoe crab (Limulus polyphemus).” The Biochemical Journal 252, no. 1 (May 1988): 151–57. https://doi.org/10.1042/bj2520151.
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    • Johnson, B. A., C. Bonaventura, and J. Bonaventura. “Allostery in Callinectes sapidus hemocyanin: cooperative oxygen binding and interactions with L-lactate, calcium, and protons.” Biochemistry 27, no. 6 (March 1988): 1995–2001. https://doi.org/10.1021/bi00406a028.
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    • Topham, R. W., S. Tesh, C. Bonaventura, and J. Bonaventura. “Active-site heterogeneity in Limulus hemocyanin as revealed by reaction with peroxides.” Archives of Biochemistry and Biophysics 261, no. 2 (March 1988): 299–311. https://doi.org/10.1016/0003-9861(88)90345-1.
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    • Johnson, B. A., J. Bonaventura, and C. Bonaventura. “Determination of L-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct homohexamers from Panulirus interruptus hemocyanin.” Biochimica Et Biophysica Acta 916, no. 3 (December 1987): 376–80. https://doi.org/10.1016/0167-4838(87)90183-x.
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    • L. Crumbliss, A., J. M. Garrison, C. R. Bock, A. Schaaf, C. J. Bonaventura, and J. Bonaventura. “Synthesis and characterization of iron(llI) chelating analogues of siderophores on organic solid supports.” Inorganica Chimica Acta 133, no. 2 (October 15, 1987): 281–87. https://doi.org/10.1016/S0020-1693(00)87780-4.
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    • Ogo, S. H., A. Focesi Júnior, R. Cashon, C. Bonaventura, and J. Bonaventura. “Fluorescence studies on the binding of reduced nicotinamide adenine dinucleotide phosphate to human hemoglobin A and its variant hemoglobin Providence.” Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Medicas E Biologicas 20, no. 6 (January 1987): 755–58.
    • Cashon, R., C. Bonaventura, J. Bonaventura, and A. Focesi. “The nicotinamide adenine dinucleotides as allosteric effectors of human hemoglobin.” The Journal of Biological Chemistry 261, no. 27 (September 1986): 12700–705. https://doi.org/10.1016/s0021-9258(18)67148-0.
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    • Fushitani, K., J. Bonaventura, and C. Bonaventura. “Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida).” Comparative Biochemistry and Physiology. B, Comparative Biochemistry 84, no. 1 (January 1986): 137–41. https://doi.org/10.1016/0305-0491(86)90283-x.
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    • Brunori, M., D. Bickar, J. Bonaventura, and C. Bonaventura. “Kinetics of reduction of cytochrome c oxidase by dithionite and the effect of hydrogen peroxide.” The Journal of Biological Chemistry 260, no. 12 (June 1985): 7165–67. https://doi.org/10.1016/s0021-9258(17)39587-x.
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    • Terwilliger, R., N. Terwilliger, C. Bonaventura, J. Bonaventura, and E. Schabtach. “Structural and functional properties of hemoglobin from the vestimentiferan Pogonophora, Lamellibrachia.” Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular 829, no. 1 (May 20, 1985): 27–33. https://doi.org/10.1016/0167-4838(85)90064-0.
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    • Bickar, D., A. Lehninger, M. Brunori, J. Bonaventura, and C. Bonaventura. “Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase.” Journal of Inorganic Biochemistry 23, no. 3–4 (March 1985): 365–72. https://doi.org/10.1016/0162-0134(85)85047-9.
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    • Kempter, B., J. Markl, M. Brenowitz, C. Bonaventura, and J. Bonaventura. “Immunological correspondence between arthropod hemocyanin subunits. II. Xiphosuran (Limulus) and spider (Eurypelma, Cupiennius) hemocyanin.” Biological Chemistry Hoppe Seyler 366, no. 1 (January 1985): 77–86. https://doi.org/10.1515/bchm3.1985.366.1.77.
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    • Bickar, D., C. Bonaventura, and J. Bonaventura. “Carbon monoxide-driven reduction of ferric heme and heme proteins.” The Journal of Biological Chemistry 259, no. 17 (September 1984): 10777–83. https://doi.org/10.1016/s0021-9258(18)90579-x.
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    • Brenowitz, M., C. Bonaventura, and J. Bonaventura. “Self-association and oxygen-binding characteristics of the isolated subunits of Limulus polyphemus hemocyanin.” Archives of Biochemistry and Biophysics 230, no. 1 (April 1984): 238–49. https://doi.org/10.1016/0003-9861(84)90105-x.
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    • Bickar, D., J. Bonaventura, C. Bonaventura, H. Auer, and M. Wilson. “Paradoxical effects of methylmercury on the kinetics of cytochrome c oxidase.” Biochemistry 23, no. 4 (February 1984): 680–84. https://doi.org/10.1021/bi00299a015.
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    • Bonaventura, C., J. Bonaventura, I. R. Hooper, and T. Marshall. “Underwater life support based on immobilized oxygen carriers.” Applied Biochemistry and Biotechnology 9, no. 1 (February 1984): 65–80. https://doi.org/10.1007/bf02798375.
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    • Brenowitz, M., C. Bonaventura, and J. Bonaventura. “Comparison of the physical and functional properties of the 48-subunit native molecule and the 24- and 12-subunit dissociation intermediates of Limulus polyphemus hemocyanin.” Biochemistry 23, no. 5 (February 1984): 879–88. https://doi.org/10.1021/bi00300a014.
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    • Johnson, B. A., C. Bonaventura, and J. Bonaventura. “Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate.” Biochemistry 23, no. 5 (February 1984): 872–78. https://doi.org/10.1021/bi00300a013.
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    • Brenowitz, M., C. Bonaventura, and J. Bonaventura. “Assembly and calcium-induced cooperativity of Limulus IV hemocyanin: a model system for analysis of structure-function relationships in the absence of subunit heterogeneity.” Biochemistry 22, no. 20 (September 1983): 4707–13. https://doi.org/10.1021/bi00289a015.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Metal ion interactions with Limulus polyphemus and Callinectes sapidus hemocyanins: stoichiometry and structural and functional consequences of calcium(II), cadmium(II), zinc(II), and mercury(II) binding.” Biochemistry 22, no. 20 (September 1983): 4713–23. https://doi.org/10.1021/bi00289a016.
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    • Brenowitz, M., J. Bonaventura, and C. Bonaventura. “Haemocyanins.” Journal of Chromatography Library 18, no. PB (January 1, 1983): 156–60. https://doi.org/10.1016/S0301-4770(08)61314-7.
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    • Bickar, D., J. Bonaventura, and C. Bonaventura. “Cytochrome c oxidase binding of hydrogen peroxide.” Biochemistry 21, no. 11 (May 1982): 2661–66. https://doi.org/10.1021/bi00540a013.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Heavy metal ion interactions with Callinectes sapidus hemocyanin: structural and functional changes induced by a variety of heavy metal ions.” Biochemistry 21, no. 10 (May 1982): 2529–38. https://doi.org/10.1021/bi00539a037.
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    • Bonaventura, J., C. Bonaventura, and M. Brouwer. “Effects of heavy metals on the respiratory proteins of marine organisms in relation to environmental pollution.” Advances in Experimental Medicine and Biology 148 (January 1982): 75–83. https://doi.org/10.1007/978-1-4615-9281-5_7.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Chloride and pH dependence of cooperative interactions in Limulus polyphemus hemocyanin.” Progress in Clinical and Biological Research 81 (January 1982): 231–56.
    • Bonaventura, C., J. Bonaventura, K. I. Miller, and K. E. Van Holde. “Hemocyanin of the chambered nautilus: structure-function relationships.” Archives of Biochemistry and Biophysics 211, no. 2 (October 1981): 589–98. https://doi.org/10.1016/0003-9861(81)90493-8.
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    • Brenowitz, M., C. Bonaventura, J. Bonaventura, and E. Gianazza. “Subunit composition of high molecular weight oligomer: Limulus polyphemus hemocyanin.” Archives of Biochemistry and Biophysics 210, no. 2 (September 1981): 748–61. https://doi.org/10.1016/0003-9861(81)90242-3.
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    • Chiancone, E., G. Ferruzzi, C. Bonaventura, and J. Bonaventura. “Amphitrite ornata erythrocruorin. II. Molecular controls of function.” Biochimica Et Biophysica Acta 670, no. 1 (August 1981): 84–92. https://doi.org/10.1016/0005-2795(81)90052-0.
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    • Markl, J., C. Bonaventura, and J. Bonaventura. “Hemocyanins in spiders, XIII. Kinetics of oxygen dissociation from individual subunits of Eurypelma and Cupiennius hemocyanin.” Hoppe Seyler’S Zeitschrift Fur Physiologische Chemie 362, no. 4 (April 1981): 429–37. https://doi.org/10.1515/bchm2.1981.362.1.429.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Effect of oxygen and allosteric effects on structural stability of oligomeric hemocyanins of the arthropod, Limulus polyphemus, and the mollusc, Helix pomatia.” Biochemistry 20, no. 7 (March 1981): 1842–48. https://doi.org/10.1021/bi00510a020.
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    • Bonaventura, J., and C. Bonaventura. “Preparation of high molecular weight invertebrate hemoglobins.” Methods in Enzymology 76 (January 1981): 43–54. https://doi.org/10.1016/0076-6879(81)76113-5.
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    • Bonaventura, C., and J. Bonaventura. “Anionic control of function in vertebrate hemoglobins.” Integrative and Comparative Biology 20, no. 1 (December 1, 1980): 131–38. https://doi.org/10.1093/icb/20.1.131.
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    • Bonaventura, J., and C. Bonaventura. “Hemocyanins relationships in their structure, function and assembly.” Integrative and Comparative Biology 20, no. 1 (December 1, 1980): 7–17. https://doi.org/10.1093/icb/20.1.7.
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    • Lamy, J., J. Bonaventura, and C. Bonaventura. “Structure, function, and assembly in the hemocyanin system of the scorpion, Androctonus australis.” Biochemistry 19, no. 13 (June 1980): 3033–39. https://doi.org/10.1021/bi00554a031.
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    • Chiancone, E., M. Brenowitz, F. Ascoli, C. Bonaventura, and J. Bonaventura. “Amphitrite ornata erythrocruorin. I. Structural properties and characterization of subunit interactions.” Biochimica Et Biophysica Acta 623, no. 1 (May 1980): 146–62. https://doi.org/10.1016/0005-2795(80)90017-3.
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    • Wilson, M. T., W. Lalla-Maharajh, V. Darley-Usmar, J. Bonaventura, C. Bonaventura, and M. Brunori. “Structural and functional properties of cytochrome c oxidases isolated from sharks.” The Journal of Biological Chemistry 255, no. 7 (April 1980): 2722–28. https://doi.org/10.1016/s0021-9258(19)85797-6.
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    • Bonaventura, C., and J. Bonaventura. “Competition in oxygen-linked anion binding to normal and variant human hemoglobins.” Hemoglobin 4, no. 3–4 (January 1980): 275–89. https://doi.org/10.3109/03630268008996210.
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    • Focesi, A., S. H. Ogo, C. Bonaventura, and J. Bonaventura. “Kinetics of oxygen and carbon monoxide binding to the hemoglobins of the water snakes Liophis miliaris and Helicops modestus.” Comparative Biochemistry and Physiology    Part B: Biochemistry And 67, no. 4 (January 1, 1980): 555–59. https://doi.org/10.1016/0305-0491(80)90414-9.
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    • Lamy, J., J. Weill, J. Bonaventura, C. Bonaventura, and M. Brenowitz. “Immunological correlates between the multiple hemocyanin subunits of Limulus polyphemus and Techypleus tridentatus.” Archives of Biochemistry and Biophysics 196, no. 2 (September 1979): 324–39. https://doi.org/10.1016/0003-9861(79)90585-x.
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    • Atha, D. H., A. Riggs, J. Bonaventura, and C. Bonaventura. “Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. pH dependence of ligand binding and subunit dissociation equilibria and kinetics.” The Journal of Biological Chemistry 254, no. 9 (May 1979): 3393–3400. https://doi.org/10.1016/s0021-9258(18)50772-9.
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    • Brouwer, M., M. Ryan, J. Bonaventura, and C. Bonaventura. “Functional and structural properties of Murex fulvescens hemocyanin: isolation of two different subunits required for reassociation of a molluscan hemocyanin.” Biochemistry 17, no. 14 (July 1978): 2810–15. https://doi.org/10.1021/bi00607a017.
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    • Weber, S. E., J. Bonaventura, B. Sullivan, and C. Bonaventura. “Oxygen equilibria and ligand-binding kinetics of erythrocruorins from two burrowing polychaetes of different modes of life, Marphysa sanguinea and Diopatra cuprea.” Journal of Comparative Physiology □ B 123, no. 2 (June 1, 1978): 177–84. https://doi.org/10.1007/BF00687847.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Analysis of the effect of three different allosteric ligands on oxygen binding by hemocyanin of the shrimp, Penaeus setiferus.” Biochemistry 17, no. 11 (May 1978): 2148–54. https://doi.org/10.1021/bi00604a019.
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    • Bucci, E., A. Salahuddin, J. Bonaventura, and C. Bonaventura. “Characterization of the ionizable groups interacting with anionic allosteric effectors of human hemoglobin.” The Journal of Biological Chemistry 253, no. 3 (February 1978): 821–27. https://doi.org/10.1016/s0021-9258(17)38177-2.
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    • Bonaventura, C., J. Bonaventura, M. Brunori, and M. Wilson. “Functional studies on crosslinked bovine cytochrome c oxidase.” Febs Letters 85, no. 1 (January 1978): 30–34. https://doi.org/10.1016/0014-5793(78)81241-1.
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    • Sekino, T., A. F. Jr, C. Bonaventura, and J. Bonaventura. “Functional properties of Aplysia brasiliana myoglobin.” Comparative Biochemistry and Physiology 61 A, no. 2 (1978): 223–26.
    • Sekino, T., A. Focesi, C. Bonaventura, and J. Bonaventura. “Purification and thermal denaturation of aplysia Brasiliana myoglobin.” Ircs Medical Science: Biochemistry 6, no. 7 (January 1, 1978): 261.
    • Amiconi, G., C. Bonaventura, J. Bonaventura, and E. Antonini. “Functional properties of normal and sickle cell hemoglobins in polyethylene glycol 6000.” Biochimica Et Biophysica Acta 495, no. 2 (December 1977): 279–86. https://doi.org/10.1016/0005-2795(77)90384-1.
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    • Moo-Penn, W. F., K. C. Bechtel, R. M. Schmidt, M. H. Johnson, D. L. Jue, D. E. Schmidt, W. M. Dunlap, S. J. Opella, J. Bonaventura, and C. Bonaventura. “Hemoglobin Raleigh (beta1 valine replaced by acetylalanine). Structural and functional characterization.” Biochemistry 16, no. 22 (November 1977): 4872–79. https://doi.org/10.1021/bi00641a019.
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    • Terwilliger, R. C., N. B. Terwilliger, C. Bonaventura, and J. Bonaventura. “Oxygen binding domains of Helisoma trivolvis hemoglobin.” Biochimica Et Biophysica Acta 494, no. 2 (October 1977): 416–25. https://doi.org/10.1016/0005-2795(77)90171-4.
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    • Brouwer, M., C. Bonaventura, and J. Bonaventura. “Oxygen binding by Limulus polyphemus hemocyanin: allosteric modulation by chloride ions.” Biochemistry 16, no. 17 (August 1977): 3897–3902. https://doi.org/10.1021/bi00636a027.
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    • Bonaventura, C., B. Sullivan, J. Bonaventura, and S. Bourne. “Anion modulation of the negative Bohr effect of haemoglobin from a primitive amphibian.” Nature 265, no. 5593 (February 1977): 474–76. https://doi.org/10.1038/265474a0.
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    • Weber, R. E., B. Sullivan, J. Bonaventura, and C. Bonaventura. “The haemoglobin systems of the bloodworms Glycera dibranchiata and G. americana. Oxygen binding properties of haemolysates and component haemoglobins.” Comparative Biochemistry and Physiology 58, no. 2 B (1977): 183–87.
    • Weber, R. E., C. Mangum, H. Steinman, C. Bonaventura, B. Sullivan, and J. Bonaventura. “Hemoglobins of two terebellid polychaetes: Enoplobranchus sanguineus and Amphitrite ornata.” Comparative Biochemistry and Physiology. A, Comparative Physiology 56, no. 2 (January 1977): 179–87. https://doi.org/10.1016/0300-9629(77)90182-7.
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    • Bonaventura, J., C. Bonaventura, B. Sullivan, G. Ferruzzi, P. R. McCurdy, J. Fox, and W. F. Moo-Penn. “Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.” The Journal of Biological Chemistry 251, no. 23 (December 1976): 7563–71. https://doi.org/10.1016/s0021-9258(17)32888-0.
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    • Sullivan, B., J. Bonaventura, C. Bonaventura, and G. Godette. “Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components.” The Journal of Biological Chemistry 251, no. 23 (December 1976): 7644–48. https://doi.org/10.1016/s0021-9258(17)32900-9.
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    • Bonaventura, C., J. Bonaventura, B. Kitto, M. Brunori, and E. Antonini. “Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber Molpadia arenicola.” Biochimica Et Biophysica Acta 428, no. 3 (May 1976): 779–86. https://doi.org/10.1016/0304-4165(76)90209-9.
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    • Weber, R. E., B. Sullivan, J. Bonaventura, and C. Bonaventura. “The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.” Biochimica Et Biophysica Acta 434, no. 1 (May 1976): 18–31. https://doi.org/10.1016/0005-2795(76)90031-3.
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    • Bonaventura, C., B. Sullivan, and J. Bonaventura. “Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost.” The Journal of Biological Chemistry 251, no. 7 (April 1976): 1871–76. https://doi.org/10.1016/s0021-9258(17)33629-3.
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    • Schwantes, A., M. L. Schwantes, C. Bonaventura, B. Sullivan, and J. Bonaventura. “Hemoglobins of Boa constrictor amarali.” Comparative Biochemistry and Physiology 54, no. 4 b (1976): 447–50.
    • Bonaventura, J., C. Bonaventura, B. Sullivan, and G. Godette. “Hemoglobin Deer Lodge (beta 2 His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.” The Journal of Biological Chemistry 250, no. 24 (December 1975): 9250–55. https://doi.org/10.1016/s0021-9258(19)40636-4.
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    • Bonaventura, J., C. Bonaventura, and B. Sullivan. “Hemoglobins and hemocyanins: comparative aspects of structure and function.” The Journal of Experimental Zoology 194, no. 1 (October 1975): 155–74. https://doi.org/10.1002/jez.1401940110.
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    • Bonaventura, C., J. Bonaventura, G. Amiconi, L. Tentori, M. Brunori, and E. Antonini. “Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.” The Journal of Biological Chemistry 250, no. 16 (August 1975): 6273–77. https://doi.org/10.1016/s0021-9258(19)41061-2.
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    • Bonaventura, J., C. Bonaventura, G. Amiconi, L. Tentori, M. Brunori, and E. Antonini. “Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg).” The Journal of Biological Chemistry 250, no. 16 (August 1975): 6278–81. https://doi.org/10.1016/s0021-9258(19)41062-4.
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    • Sullivan, B., J. Bonaventura, C. Bonaventura, L. Pennell, J. Elliott, R. Boyum, and W. Lambie. “The structure and evolution of parvalbumins. I. Amino acid compositional studies of parvalbumins from four perciform species.” Journal of Molecular Evolution 5, no. 2 (July 1975): 103–16. https://doi.org/10.1007/bf01732515.
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    • Mangum, C. P., B. R. Woodin, and C. Bonaventura. “The role of coelomic and vascular hemoglobin in the annelid family Terebellidae.” Comparative Biochemistry and Physiology 51, no. 2 a (1975): 281–94.
    • Bonaventura, C., B. Sullivan, J. Bonaventura, and S. Bourne. “CO binding by hemocyanins of Limulus polyphemus, Busycon carica, and Callinectes sapidus.” Biochemistry 13, no. 23 (November 1974): 4784–89. https://doi.org/10.1021/bi00720a016.
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    • Bonaventura, J., C. Bonaventura, and B. Sullivan. “Hemoglobin of the electric Atlantic torpedo, Torpedo nobiliana: a cooperative hemoglobin without Bohr effects.” Biochimica Et Biophysica Acta 371, no. 1 (November 1974): 147–54. https://doi.org/10.1016/0005-2795(74)90163-9.
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    • Bonaventura, J., C. Bonaventura, and B. Sullivan. “Urea tolerance as a molecular adaptation of elasmobranch hemoglobins.” Science (New York, N.Y.) 186, no. 4158 (October 1974): 57–59. https://doi.org/10.1126/science.186.4158.57.
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    • Sullivan, B., J. Bonaventura, and C. Bonaventura. “Functional differences in the multiple hemocyanins of the horseshoe crab, Limulus polyphemus L.” Proceedings of the National Academy of Sciences of the United States of America 71, no. 6 (June 1974): 2558–62. https://doi.org/10.1073/pnas.71.6.2558.
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    • Bonaventura, C., B. Sullivan, and J. Bonaventura. “Effect of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus.” The Journal of Biological Chemistry 249, no. 12 (June 1974): 3768–75. https://doi.org/10.1016/s0021-9258(19)42540-4.
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    • Tondo, C., J. Bonaventura, C. Bonaventura, M. Brunori, G. Amiconi, and E. Antonini. “Functional properties of hemoglobin Pôrto Alegre (alpha2A beta2 9Ser leads to Cys) and the reactivity of its extra cysteinyl residue.” Biochimica Et Biophysica Acta 342, no. 1 (March 1974): 15–20. https://doi.org/10.1016/0005-2795(74)90101-9.
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    • Bonaventura, J., C. Bonaventura, M. Brunori, B. Giardina, E. Antonini, F. Bossa, and J. Wyman. “Functional properties of carboxypeptidase-digested hemoglobins.” Journal of Molecular Biology 82, no. 4 (February 1974): 499–511. https://doi.org/10.1016/0022-2836(74)90244-7.
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    • Bonaventura, J., C. Bonaventura, and G. Amiconi. “Functional properties of hemoglobin Leiden (α2(A)β2(6 or 7 Glu deleted)).” Archives of Biochemistry and Biophysics 161, no. 1 (1974): 328–32.
    • Bonaventura, C., J. Bonaventura, E. Antonini, M. Brunori, and J. Wyman. “Carbon monoxide binding by simple heme proteins under photodissociating conditions.” Biochemistry 12, no. 18 (August 1973): 3424–28. https://doi.org/10.1021/bi00742a010.
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    • Brunori, M., J. Bonaventura, C. Bonaventura, B. Giardina, F. Bossa, and E. Antonini. “Hemoglobins from trout: structural and functional properties.” Molecular and Cellular Biochemistry 1, no. 2 (June 1973): 189–96. https://doi.org/10.1007/bf01659329.
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    • Wilson, M. T., M. Brunori, J. Bonaventura, and C. Bonaventura. “Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c.” The Biochemical Journal 131, no. 4 (April 1973): 863–65. https://doi.org/10.1042/bj1310863.
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    • Bonaventura, J., C. Bonaventura, B. Giardina, E. Antonini, M. Brunori, and J. Wyman. “Partial restoration of normal functional properties in carboxypeptidase A-digested hemoglobin.” Proceedings of the National Academy of Sciences of the United States of America 69, no. 8 (August 1972): 2174–78. https://doi.org/10.1073/pnas.69.8.2174.
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    • Brunori, M., J. Bonaventura, C. Bonaventura, E. Antonini, and J. Wyman. “Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.” Proceedings of the National Academy of Sciences of the United States of America 69, no. 4 (April 1972): 868–71. https://doi.org/10.1073/pnas.69.4.868.
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    • Bonaventura, C., and M. Kindergan. “Kinetic and spectral resolution of two components of delayed emission from Chlorella pyrenoidosa.” Bba  Bioenergetics 234, no. 2 (1971): 249–65.
    • Bonaventura, C., and J. Myers. “Fluorescence and oxygen evolution from Chlorella pyrenoidosa.” Bba  Bioenergetics 189, no. 3 (1969): 366–83.

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