Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1984-4-10
pubmed:abstractText
Reduction and reoxidation of beef heart cytochrome oxidase, under conditions that ensure the strict absence of hydrogen peroxide, produce a fully oxidized form of the enzyme that has the Soret band at 420 nm, as opposed to the 428 nm band normally associated with the pulsed or oxygenated enzyme. The 420 nm form shows the enhancement of catalytic activity associated with the pulsed enzyme. Addition of hydrogen peroxide to the 420 nm form gives rise to the 428 nm band of the oxygenated enzyme, thereby clearly establishing that the 428 nm form is a peroxide derivative of the fully oxidized enzyme. Previous data from other groups are re-evaluated in the light of our experiments.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2073-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The identity of pulsed cytochrome oxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't