Reaction of Caa3-type Terminal Cytochrome Oxidase from the Thermophilic Bacterium PS3 with Oxygen and Carbon Monoxide at Low Temperatures

Overview

Journal Biochem J

Specialty Biochemistry

Date 1984 Jul 15

PMID 6089742

Citations 3

Authors

N Sone

A Naqui

C Kumar

B Chance

Affiliations

Soon will be listed here.

Abstract

Reaction of O2 and CO with a caa3-type terminal cytochrome oxidase (EC 1.9.3.1) from the thermophilic bacterium PS3 grown with high aeration was studied at low temperatures. The CO recombination at the temperature range studied (-50 degrees C to -80 degrees C) followed first-order kinetics with an activation energy of 29.3 kJ/mol (7.0 kcal/mol). In the presence of O2 at -113 degrees C the photolysed reduced form binds O2 to form an 'oxy' intermediate similar to Compound A. At a higher temperature (-97 degrees C) another intermediate, similar to Compound B, is formed as a result of electron transfer from the enzyme to the liganded O2.

Citing Articles

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.

Pulsed cytochrome c oxidase from the thermophilic bacterium PS3.

Sone N, Naqui A, Kumar C, Chance B Biochem J. 1984; 223(3):809-13.

PMID: 6095810 PMC: 1144366. DOI: 10.1042/bj2230809.

Evidence for dimer structure of proton-pumping cytochrome c oxidase, an analysis by radiation inactivation.

Sone N, Kosako T EMBO J. 1986; 5(7):1515-9.

PMID: 3017697 PMC: 1166974. DOI: 10.1002/j.1460-2075.1986.tb04391.x.

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