Low-temperature Kinetics of the Reaction of Oxygen and Solubilized Cytochrome Oxidase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1978 Jun 1

PMID 208516

Citations 15

Authors

B Chance

C Saronio

J S Leigh Jr

W J Ingledew

T E King

Affiliations

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Abstract

The reaction of solubilized cytochrome oxidase in the fully reduced state with O2 at low temperatures reveals components with characteristics similar to those observed with the membrane-bound oxidase, namely compounds A and B, which are proposed to be 'oxy' and 'peroxy' compounds respectively. Similar species are identified in both solubilized and membrane-bound oxidases; the reaction velocity constant for the reation with O2 and the dissociation constant are decreased 2-3-fold in the solubilied preparation as compared with the membrane-bound species, owing to decreased reactivity towards O2 in the former. The oxidase prepared in the mixed-valence state shows the distinctive absorption band characteristic of compound C, identified in the membrane-bound oxidase. The assignment of the alpha, beta, gamma and near-i.r. absorption bands to possible valence states of these compounds is made.

Citing Articles

Reaction of Mixed Valence State Cytochrome Oxidase with Oxygen in Plant Mitochondria: A STUDY BY LOW TEMPERATURE FLASH PHOTOLYSIS AND RAPID WAVELENGTH SCANNING OPTICAL SPECTROMETRY.

Denis M, Clore G Plant Physiol. 1981; 68(1):229-35.

PMID: 16661874 PMC: 425919. DOI: 10.1104/pp.68.1.229.

Carbon monoxide- and oxygen-reacting haemoproteins in the mitochondrial fraction from the soil amoeba Acanthamoeba castellanii. Studies at subzero temperatures.

Lloyd D, Edwards S, Chance B Biochem J. 1981; 200(2):337-42.

PMID: 7340835 PMC: 1163540. DOI: 10.1042/bj2000337.

Characterization of the intermediates in the reaction of membrane-bound mixed-valence-state cytochrome oxidase with oxygen at low temperatures by optical spectroscopy in the visible region.

Clore G Biochem J. 1980; 187(3):617-22.

PMID: 6331384 PMC: 1162444. DOI: 10.1042/bj1870617.

The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.

Hill B, Greenwood C Biochem J. 1984; 218(3):913-21.

PMID: 6326750 PMC: 1153423. DOI: 10.1042/bj2180913.

Structural features and the reaction mechanism of cytochrome oxidase: iron and copper X-ray absorption fine structure.

Powers L, Chance B, Ching Y, Angiolillo P Biophys J. 1981; 34(3):465-98.

PMID: 6264990 PMC: 1327488. DOI: 10.1016/S0006-3495(81)84863-1.

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