Heme-Heme Orientation and Electron Transfer Kinetic Behavior of Multisite Oxidation-Reduction Enzymes
Author:
Affiliation:
1. Department of Biophysics and Theoretical Biology, University of Chicago, Cummings Life Science Center, Chicago, Illinois 60637
2. Arthur Amos Noyes Laboratory, California Institute of Technology, Pasadena 91125
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference33 articles.
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2. CHURG, A.K., CORRECTION, JOURNAL OF CHEMICAL PHYSICS 69: 2268 (1978).
3. CHURG, A.K., ELECTRONIC-STRUCTURE AND COORDINATION GEOMETRY OF OXYHEME COMPLEX IN MYOGLOBIN, JOURNAL OF CHEMICAL PHYSICS 68: 1913 (1978).
4. EATON, W.A., ELECTRONIC SPECTRUM OF SINGLE CRYSTALS OF FERRICYTOCHROME-C, JOURNAL OF CHEMICAL PHYSICS 46: 2533 (1967).
5. EATON, W.A., SINGLE-CRYSTAL SPECTRA OF FERRIMYOGLOBIN COMPLEXES IN POLARIZED LIGHT, JOURNAL OF CHEMICAL PHYSICS 49: 985 (1968).
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