Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability.

Abstract:

:Cytochrome bd is one of the two terminal ubiquinol oxidases in the respiratory chain of Escherichia coli catalyzing reduction of O2 to H2O. The enzyme is expressed under low oxygen tension; due to high affinity for O2 it is isolated mainly as a stable oxygenated complex. Direct measurement of O2 binding to heme d in the one-electron reduced isolated enzyme gives K(d(O2)) of approximately 280 nM. It is possible to photolyse the heme d oxy-complex by illumination of the enzyme for several minutes under microaerobic conditions; the light-induced difference absorption spectrum is virtually identical to the inverted spectrum of O2 binding to heme d.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Belevich I,Borisov VB,Konstantinov AA,Verkhovsky MI

doi

10.1016/j.febslet.2005.07.011

keywords:

subject

Has Abstract

pub_date

2005-08-29 00:00:00

pages

4567-70

issue

21

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00854-9

journal_volume

579

pub_type

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