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| Hemoglobins Objective: To investigate the redox chemistry of wild type and mutant hemoglobins and myoglobins in relation to O2 and NO transport and storage functions, and allosteric control. |
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Difference in Redox Behavior Due to Heme Environment, and Allosteric, and Thiosteric Effects |
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See for example: “Anaerobic Oxidations of Myoglobin and Hemoglobin Using Spectroelectrochemistry” C. H. Taboy, C. Bonaventura and A. L. Crumbliss, Methods in Enzymology – Redox Cell Biology & Genetics, C. K. Sen and L. Packer, Volume Eds., J. N. Abelson and M I. Simon, Eds.-In-Chief, Academic Press, NY, p. 187, 2002. “Critical Redox and Allosteric Aspects of Nitric Oxide Interactions with Hemoglobin” C. Bonaventura, A. Fago, R. W. Henkens and A. L. Crumbliss, Antioxidants & Redox Signaling, 6, 979 (2004). |
Last update January 2005
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