Heme proteins and metalloporphyrins: Redox chemistry and oxygen binding
Article first published online: 19 OCT 2004
Copyright © 1979 John Wiley & Sons, Inc.
International Journal of Quantum Chemistry
Volume 16, Issue 2, pages 311–329, August 1979
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
- Issue published online: 19 OCT 2004
- Article first published online: 19 OCT 2004
- Manuscript Accepted: 29 JAN 1979
- Manuscript Received: 23 OCT 1978
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.