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Kinetics of CO binding to H(+)-motive oxidases of the caa3-type from Bacillus FTU and of the o-type from Escherichia coli.

作者信息

Muntyan M S, Bloch D A, Ustiyan V S, Drachev L A

机构信息

A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.

出版信息

FEBS Lett. 1993 Aug 2;327(3):351-4. doi: 10.1016/0014-5793(93)81019-v.

DOI:10.1016/0014-5793(93)81019-v
PMID:8348963
Abstract

The kinetics of CO rebinding with isolated Bacillus FTU caa3-type oxidase and with solubilized Escherichia coli membranes (GO103 strain) containing the o-type oxidase as the main O2-reducing enzyme were studied under reducing conditions by laser flash photolysis of the CO-oxidase complexes. The spectra of the optical absorbance changes upon photolysis were characteristic of CO-caa3- and CO-o-oxidase complexes in Bac. FTU and E. coli, respectively. Small quantities of d-type oxidase in E. coli GO103 membranes were detected. The kinetics of CO reassociation with reduced caa3- and o-type oxidases were monophasic with tau 25-30 ms in both cases.

摘要

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