Abstract
Heme containing proteins function as oxygen carriers, electron carriers or enzymes in biological systems. Of particular interest to this investigation is the ability of heme proteins to serve as electron carriers. The heme group, an iron atom bound to the four nitrogens of a porphyrin ring system, is the characteristic structural feature in common to all heme proteins. The iron atom serves as the site of oxidation or reduction during electron transfer. However, heme proteins exhibit significantly different thermodynamic and kinetic properties for electron transfer reactions. These differences between heme proteins must be due to the protein structure and the location of the heme group within the molecule. Although hemoglobin functions physiologically as an oxygen carrier rather than an electron carrier it is an ideal molecule to use as a model for the study of the electron transfer reactions of heme proteins. This is because it is readily available, has a moderate cost and has a known and documented structure.
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Detrich, J.L., Erb, G.A., Beres, D.A., Rickard, L.H. (1992). Thermodynamic and Electrochemical Studies of the Electron Transfer Reactions of Hemoglobin. In: Allen, M.J., Cleary, S.F., Sowers, A.E., Shillady, D.D. (eds) Charge and Field Effects in Biosystems—3. Birkhäuser Boston. https://doi.org/10.1007/978-1-4615-9837-4_4
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DOI: https://doi.org/10.1007/978-1-4615-9837-4_4
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