Article
Heme proteins and metalloporphyrins: Redox chemistry and oxygen binding
Article first published online: 19 OCT 2004
DOI: 10.1002/qua.560160213
Copyright © 1979 John Wiley & Sons, Inc.
Additional Information
How to Cite
Dolphin, D., Addison, A. W., Cairns, M., Dinello, R. K., Farrell, N. P., James, B. R., Paulson, D. R. and Welborn, C. (1979), Heme proteins and metalloporphyrins: Redox chemistry and oxygen binding. Int. J. Quantum Chem., 16: 311–329. doi: 10.1002/qua.560160213
Publication History
- Issue published online: 19 OCT 2004
- Article first published online: 19 OCT 2004
- Manuscript Accepted: 29 JAN 1979
- Manuscript Received: 23 OCT 1978
- Abstract
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Abstract
Metalloporphyrins perform a variety of functions in nature from the storage and transport of electrons and molecular oxygen to the decomposition of hydrogen peroxide and the activation of oxygen. The chemistry of both the centrally coordinated metal and the porphyrin macrocycle play important roles in these reactions. The use of model systems and metalloporphyrins, other than iron porphyrins, is described for the elucidation of the mechanism of action of the natural systems.

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