Single electron reduction of 'slow' and 'fast' cytochrome-c oxidase.

Abstract:

:Evidence is presented that single electron reduction is sufficient for rapid electron transfer (k greater than 20 s-1 at pH 8.0 in 0.43 M potassium EDTA) between haem a/CuA and the binuclear centre in 'fast' oxidase, whereas in 'slow' oxidase intramolecular electron transfer is slow even when both CuA and haem a are reduced (k congruent to 0.01 s-1). However, while a single electron can equilibrate rapidly between CuA, haem a and CuB in 'fast' oxidase, it seems that equilibration with haem a3 is relatively slow (k congruent to 2 s-1). Electron transfer between cytochrome c and CuA/haem a is similar for both types of enzyme (k congruent to 2.4 x 10(5) M-1.s-1).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Moody AJ,Brandt U,Rich PR

doi

10.1016/0014-5793(91)81161-z

subject

Has Abstract

pub_date

1991-11-18 00:00:00

pages

101-5

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)81161-Z

journal_volume

293

pub_type

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