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Flow-flash kinetics of O2 binding to cytochrome c oxidase at elevated [O2]: observations using high pressure stopped flow for gaseous reactants.

Abstract：

:A high-pressure stopped-flow apparatus developed in our laboratories provides the capability to use dissolved gaseous reactants at elevated concentrations in solution (in equilibrium with gas pressures up to ca. 30 atm) for measurement of reaction kinetics. We have used this apparatus to follow the reaction of dioxygen with bovine cytochrome c oxidase following photolysis of the fully reduced CO ligated enzyme up to a dioxygen concentration of 16 mM. The observed rate dependence on [02] follows saturation kinetics and was fit to a limiting rate of 1.0 X 10(6) s(-1). This value is approximately the same as that for the thermal loss of CO to solution from the transient CuB bound state formed upon photolysis of the heme-CO complex. Implications for the mechanism of O2 binding and reduction by the heme-copper oxidases are discussed.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bailey JA,James CA,Woodruff WH

doi

10.1006/bbrc.1996.0531

subject

Has Abstract

pub_date

1996-03-27 00:00:00

pages

1055-60

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)90531-8

journal_volume

220

pub_type

杂志文章

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