Kinetics of CO binding to H(+)-motive oxidases of the caa3-type from Bacillus FTU and of the o-type from Escherichia coli.
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.
Muntyan
M S
MS
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.
Bloch
D A
DA
Ustiyan
V S
VS
Drachev
L A
LA
D001407:Bacillus / Q000201:enzymology*; D002248:Carbon Monoxide / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006859:Hydrogen / Q000378:metabolism*; D007700:Kinetics; D010088:Oxidoreductases / Q000378:metabolism*; D010782:Photolysis; D013057:Spectrum Analysis
D002248:Carbon Monoxide; D006859:Hydrogen; D010088:Oxidoreductases