Kinetics of CO binding to H+‐motive oxidases of the caa 3‐type from Bacillus FTU and of the o‐type from Escherichia coli

FEBS Letters

Muntyan, M.S.¹  Bloch, D.A.¹  Drachev, L.A.¹  Ustiyan, V.S.¹ 

[1] A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899 Moscow, Russian Federation

关键词: Flash photolysis;    caa 3Type oxidase;    o-Type oxidase;    Bacillus FTU;    Escherichia coli;    TMPD;    N;    N;    N'N'-tetramethyl-p-phenylendiamine;    PAG;    polyacrylamide gel;    Δ̃smH +;    the proton electrochemical gradient;   

DOI  :  10.1016/0014-5793(93)81019-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 O₂reducing 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.

【 授权许可】

Unknown