Cytochrome Caa3 from the Thermophilic Bacterium Thermus Thermophilus: a Member of the Heme-copper Oxidase Superfamily

Overview

Journal J Bioenerg Biomembr

Publisher Springer

Specialties Biochemistry
Biology
Endocrinology

Date 1993 Apr 1

PMID 8389743

Citations 5

Authors

J A Fee

T Yoshida

K K Surerus

M W Mather

Affiliations

Soon will be listed here.

Abstract

The subject of this short review is the cytochrome c oxidase (caa3) from the thermophilic bacterium Thermus thermophilus. First, some of the extensive physical and enzymological results obtained with this enzyme are reviewed, and two experiments are described, involving isotope substitutions in combination with Mössbauer and ENDOR spectroscopies, which have provided novel insight into the active sites of the enzyme. Second, we summarize recent molecular genetic work showing that Thermus cytochrome caa3 is a bona fide member of the superfamily of heme-copper oxidases. Finally, we present a rough three-dimensional model and speculate about certain features of the metal-binding sites.

Citing Articles

A novel heme a insertion factor gene cotranscribes with the Thermus thermophilus cytochrome ba3 oxidase locus.

Werner C, Richter O, Ludwig B J Bacteriol. 2010; 192(18):4712-9.

PMID: 20622059 PMC: 2937409. DOI: 10.1128/JB.00548-10.

Thermus thermophilus as biological model.

Cava F, Hidalgo A, Berenguer J Extremophiles. 2009; 13(2):213-31.

PMID: 19156357 DOI: 10.1007/s00792-009-0226-6.

Molecular mechanism of energy conservation in polysulfide respiration.

Jormakka M, Yokoyama K, Yano T, Tamakoshi M, Akimoto S, Shimamura T Nat Struct Mol Biol. 2008; 15(7):730-7.

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A flash-photolysis study of the reactions of a caa3-type cytochrome oxidase with dioxygen and carbon monoxide.

Hirota S, Adelroth P, Sone N, Nilsson T, Malmstrom B, Brzezinski P J Bioenerg Biomembr. 1996; 28(6):495-501.

PMID: 8953381 DOI: 10.1007/BF02110439.

The superfamily of heme-copper respiratory oxidases.

Garcia-Horsman J, Barquera B, Rumbley J, Ma J, Gennis R J Bacteriol. 1994; 176(18):5587-600.

PMID: 8083153 PMC: 196760. DOI: 10.1128/jb.176.18.5587-5600.1994.

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