Temperature dependence of the reduction potential of CuA in carbon monoxide inhibited cytochrome c oxidase.

Abstract:

:The temperature dependence of the reduction potential of the CuA site in carbon monoxide inhibited cytochrome c oxidase has been measured with a spectroelectrochemical method adapted to the relatively weak near-infrared absorption of this copper ion. These measurements, together with parallel measurements on the 604-nm absorption due to Fea, indicate that an interaction between CuA and Fea causes the reduction potential for one of these sites to be decreased by approximately 40 mV upon reduction of the other. The temperature dependence of the CuA reduction potential indicates a relatively large and negative standard entropy of reduction of CuA (delta So' = -48.7 +/- 2.3 eu). Possible implications of the intersite redox interaction and the large standard entropy of reduction of the CuA site are discussed.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wang H,Blair DF,Ellis WR Jr,Gray HB,Chan SI

doi

10.1021/bi00349a024

subject

Has Abstract

pub_date

1986-01-14 00:00:00

pages

167-71

issue

1

eissn

0006-2960

issn

1520-4995

journal_volume

25

pub_type

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