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

Autor: Muntyan MS; A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation., Bloch DA, Ustiyan VS, Drachev LA
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 1993 Aug 02; Vol. 327 (3), pp. 351-4.
DOI: 10.1016/0014-5793(93)81019-v
Abstrakt: 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.
Databáze: MEDLINE