The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin.

Abstract

I. Introduction II. Dynamics of the FeO2 Bonding of Myoglobin and Hemoglobin in Vivo III. Dioxygen Pressure Dependence of the Autoxidation Rate: An Outer-Sphere Electron Transfer Mechanism IV. Effects of pH on the Autoxidation Rate: An Inner-Sphere Electron Transfer Mechanism A. Unimolecular, Spontaneous Dissociation of O2- from the FeO2 Center in Mb and Hb B. Various Types of pH Profiles for the Autoxidation Rate of Oxymyoglobins: A Comparative Study C. A Complete Kinetic Formulation for the pH Dependence D. Bimolecular Displacement of O2- from the FeO2 Center by Nucleophiles: An SN2 Mechanism V. Subsequent Side Reactions in the Autoxidation of Oxymyoglobin: An Overall Stoichiometry VI. Role of the Globin Moiety in Stabilizing the FeO2 Bonding in Myoglobin VII. Conclusion VIII. Acknowledgments IX. References