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Kinetics of CO binding to H + ‐motive oxidases of the caa 3 ‐type from Bacillus FTU and of the o ‐type from Escherichia coli
Author(s) -
Muntyan M.S.,
Bloch D.A.,
Ustiyan V.S.,
Drachev L.A.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81019-v
Subject(s) - kinetics , chemistry , escherichia coli , flash photolysis , oxidase test , membrane , absorbance , photodissociation , enzyme , strain (injury) , biochemistry , chromatography , photochemistry , reaction rate constant , biology , physics , quantum mechanics , gene , anatomy
The kinetics of CO rebinding with isolated Bacillus FTU caa 3 ‐type oxidase and with solubilized Escherichia coli membranes (GO103 strain) containing the o ‐type oxidase as the main O 2 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‐ caa 3 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 caa 3 and o ‐type oxidases were monophasic with τ 25–30 ms in both cases.