Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-5-20
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1055-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Flow-flash kinetics of O2 binding to cytochrome c oxidase at elevated [O2]: observations using high pressure stopped flow for gaseous reactants.
pubmed:affiliation
Biosciences and Biotechnology Group, Los Almos National Library, New Mexico 87545, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.