KINETICS OF CO BINDING TO H-MOTIVE OXIDASES OF THE CAA3-TYPE FROM BACILLUS FTU AND OF THE O-TYPE FROM ESCHERICHIA-COLI()

Citation
Ms. Muntyan et al., KINETICS OF CO BINDING TO H-MOTIVE OXIDASES OF THE CAA3-TYPE FROM BACILLUS FTU AND OF THE O-TYPE FROM ESCHERICHIA-COLI(), FEBS letters, 327(3), 1993, pp. 351-354
Citations number
25
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
327
Issue
3
Year of publication
1993
Pages
351 - 354
Database
ISI
SICI code
0014-5793(1993)327:3<351:KOCBTH>2.0.ZU;2-F
Abstract
The kinetics of CO rebinding with isolated Bacillus FTU caa3-type oxid ase and with solubilized Escherichia coli membranes (GO103 strain) con taining 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 photoly sis 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.