A cytochrome o-type oxidase of the thermophilic bacterium PS3 grown under air-limited conditions.

Abstract:

:A cytochrome o-type oxidase from the thermophilic bacterium PS3 grown under air-limited conditions was purified by ion-exchange chromatography in the presence of a non-ionic detergent. The enzyme was composed of three subunits (60, 30, and 16 kDa) and seemed to contain two molecules of heme b as prosthetic groups. It contained no detectable copper. The reduced enzyme showed absorption bands at 426 and 558.5 nm, and a characteristic spectral change upon binding CO. It oxidized several cytochromes c and artificial dyes such as N,N,N',N'-tetramethyl-p-phenylenediamine and phenazonium methosulfate at appreciable rates. Its Km for O2 was low (0.09 microM). It was capable of transmembrane electron transfer, because when reconstituted into liposomes, it generated a membrane potential upon oxidation without pumping protons.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Sone N,Kutoh E,Sato K

doi

10.1093/oxfordjournals.jbchem.a123092

subject

Has Abstract

pub_date

1990-04-01 00:00:00

pages

597-602

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

107

pub_type

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