Intramolecular electron transfer processes in Cu(B)-deficient cytochrome bo studied by pulse radiolysis.

Abstract:

:The Escherichia coli cytochrome bo is a heme-copper terminal ubiquinol oxidase, and functions as a redox-driven proton pump. We applied pulse radiolysis technique for studying the one-electron reduction processes in the Cu(B)-deficient mutant, His333Ala. We found that the Cu(B) deficiency suppressed the heme b-to-heme o electron transfer two order of the magnitude (4.0 x 10(2) s(-1)), as found for the wild-type enzyme in the presence of 1 mM KCN (3.0 x 10(2) s(-1)). Potentiometric analysis of the His333Ala mutant revealed the 40 mV decrease in the E(m) value for low-spin heme b and the 160 mV increase in the E(m) value of high-spin heme o. Our results indicate that Cu(B) not only serves as one-electron donor to the bound dioxygen upon the O-O bond cleavage, but also facilitates dioxygen reduction at the heme-copper binuclear centre by modulating the E(m) value of heme o through magnetic interactions. And the absence of a putative OH(-) bound to Cu(B) seems not to affect the uptake of the first chemical proton via K-channel in the His333Ala mutant.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Kobayashi K,Tagawa S,Mogi T

doi

10.1093/jb/mvp026

subject

Has Abstract

pub_date

2009-05-01 00:00:00

pages

685-91

issue

5

eissn

0021-924X

issn

1756-2651

pii

mvp026

journal_volume

145

pub_type

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