A New High Potential Redox Transition for Cytochrome Aa3

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1988 Jul 1

PMID 2843243

Citations 4

Authors

R W Hendler

G S Sidhu

Affiliations

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Abstract

Using cyano-complexes of iron, tungsten, and molybdenum and a platinum working electrode, we have been able to attain and hold voltages in the range of 400 to 900 mV (vs. standard hydrogen electrode) in an aqueous medium. With this system we have obtained additional information in support of an earlier conclusion that cytochrome a3 has a high Em transition (i.e. greater than 460 mV) in addition to its Em in the 180-200 mV range (Hendler, R. W., K. V. S. Reddy, R. I. Shrager, and W. S. Caughey. 1986. Biophys. J. 49:717-729; Reddy, K. V. S., and R. W. Hendler. 1986. Biophys. J. 49:693-703). The proposed new transition has an Em near 770 mV and an n value greater than 1. The reduced form of the high-potential species of cytochrome a3 does not bind CO, in contrast to the reduced form of the low-potential species which does. A possible reaction scheme for cytochrome aa3 which incorporates the new information is presented.

Citing Articles

High voltage redox properties of cytochrome c oxidase.

Hendler R, Sidhu G, Pardhasaradhi K Biophys J. 1990; 58(4):957-67.

PMID: 2174273 PMC: 1281041. DOI: 10.1016/S0006-3495(90)82440-1.

Characterization of two low Em forms of cytochrome a3 and their carbon monoxide complexes in mammalian cytochrome c oxidase.

Sidhu G, Hendler R Biophys J. 1990; 57(6):1125-40.

PMID: 2168220 PMC: 1280824. DOI: 10.1016/S0006-3495(90)82633-3.

Potentiometric and spectral studies with the two-subunit cytochrome aa3 from Paracoccus denitrificans. Comparison with the 13-subunit beef heart enzyme.

Pardhasaradhi K, Ludwig B, Hendler R Biophys J. 1991; 60(2):408-14.

PMID: 1655082 PMC: 1260077. DOI: 10.1016/S0006-3495(91)82066-5.

Redox interactions in cytochrome c oxidase: from the "neoclassical" toward "modern" models.

Hendler R, Westerhoff H Biophys J. 1992; 63(6):1586-604.

PMID: 1336989 PMC: 1262276. DOI: 10.1016/S0006-3495(92)81748-4.

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