Linked Life Data

1846351

Source:http://linkedlifedata.com/resource/pubmed/id/1846351

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-2-27
pubmed:abstractText
We report here extensive and accurate analyses of the copper, iron, zinc, and magnesium contents in bovine heart cytochrome c oxidase by direct current plasma atomic emission spectrometry. The precision of an individual measurement is within +/- 5%. The analyses confirm a stoichiometry of 5Cu/4Fe/2Zn/2Mg per dimer. Seven enzyme preparations treated by various methods are also analyzed to investigate the nature of Cux. It is shown that Cux is removable by either monomerization of the enzyme or subunit III depletion. This result suggests that Cux is associated with subunit III and that it plays a structural role in enzyme dimerization. EPR measurements indicate that Cux is heterogeneous and mostly reduced. In addition, we find Cux has no effect on the spectroscopic properties and electron transfer activity of the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1367-70
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The nature of Cux in cytochrome c oxidase.
pubmed:affiliation
A. A. Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't