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Science 15 April 1988:
Vol. 240. no. 4850, pp. 311 - 313
DOI: 10.1126/science.2832950
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Articles

Science, Vol 240, Issue 4850, 311-313
Copyright © 1988 by American Association for the Advancement of Science

articles

Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

N Liang, AG Mauk, GJ Pielak, JA Johnson, M Smith, and BM Hoffman

Department of Chemistry, Northwestern University, Evanston, IL 60208.

Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is approximately 10(4) slower at approximately 0 degrees C than for the two variants with aromatic residues.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Electron-Tunneling Pathways in Cytochrome c.
D. S. Wuttke, M. J. Bjerrum, J. R. Winkler, and H. B. Gray (1992)
Science 256, 1007-1009
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