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Electron transfer between cytochromec and cytochromec peroxidase

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Abstract

The reaction between cytochromec (CC) and cytochromec peroxidase (CcP) is a very attractive system for investigating the fundamental mechanism of biological electron transfer. The resting ferric state of CcP is oxidized by hydrogen peroxide to compound I (CMPI) containing an oxyferryl heme and an indolyl radical cation on Trp-191. CMPI is sequentially reduced to CMPII and then to the resting state CcP by two molecules of CC. In this review we discuss the use of a new ruthenium photoreduction technique and other rapid kinetic techniques to address the following important questions: (1) What is the initial electron acceptor in CMPI? (2) What are the true rates of electron transfer from CC to the radical cation and to the oxyferryl heme? (3) What are the binding domains and pathways for electron transfer from CC to the radical cation and the oxyferryl heme? (4) What is the mechanism for the complete reaction under physiological conditions?

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Abbreviations

CC:

cytochrome c

hCC:

horse CC

yCC:

yeast iso-1-CC

CcP:

cytochrome c peroxidase

CMPI:

CcP compound I

Ru-27-hCC:

Ru(bipyridine)2(4-methyl, 4′-carboxybipyridine-lysine-27-cytochrome c)

Ru-39-yCC:

Ru(bpy)2(4,4′-dimethylbi-pyridine-Cys-39-yeast-iso-1-cytochrome c)

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of Arkansas, 72701, Fayetteville, Arkansas

    Francis Millett, Lois Geren & Bill Durham

  2. Department of Chemistry, University of California at San Diego, 92093, La Jolla, California

    Mark A. Miller

Authors
  1. Francis Millett
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  2. Mark A. Miller
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  3. Lois Geren
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  4. Bill Durham
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Millett, F., Miller, M.A., Geren, L. et al. Electron transfer between cytochromec and cytochromec peroxidase. J Bioenerg Biomembr 27, 341–351 (1995). https://doi.org/10.1007/BF02110103

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  • DOI: https://doi.org/10.1007/BF02110103

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