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

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 caa 3-type oxidase and with solubilized Escherichia coli membranes (GO103 strain) containing the o-type oxidase as the main O 2reducing enzyme were studied under reducing conditions by laser flash photolysis of the CO-oxidase complexes. The spe...

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Veröffentlicht in:FEBS letters 1993-08, Vol.327 (3), p.351-354
Hauptverfasser: Muntyan, M.S., Bloch, D.A., Ustiyan, V.S., Drachev, L.A.
Format: Artikel
Sprache:eng
Schlagworte:
Bacillus - enzymology
Bacillus FTU
caa3Type oxidase
Carbon Monoxide - metabolism
Escherichia coli
Escherichia coli - enzymology
Flash photolysis
Hydrogen - metabolism
Kinetics
o-Type oxidase
Oxidoreductases - metabolism
Photolysis
Spectrum Analysis
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Zusammenfassung: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 2reducing 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)81019-V