Linked Life Data

3029102

Source:http://linkedlifedata.com/resource/pubmed/id/3029102

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1987-4-17
pubmed:abstractText
The structures of membrane proteins are difficult to obtain by crystallography and may be altered by the detergents used in their extraction. X-ray absorption spectroscopy has been used to identify the structures of the copper atoms of the membrane-bound enzyme in mitochondria and in submitochondrial particles at respective concentrations of 100 and 200 micron of molar copper. To within the experimental error, the x-ray absorption spectra of the copper atoms of the membrane-bound and the Yonetani (Yonetani, T. (1961) J. Biol. Chem. 236, 1680-1688) purified oxidase are identical; all detectable shells of the active site indicate no alteration of structural parameters. Significant differences are found when compared to the Hartzell-Beinert (Hartzell, R. C., and Beinert, H. (1974) Biochim. Biophys. Acta 368, 318-338) preparation. Extended x-ray absorption fine structure technology is now adequate for the direct studies of membrane proteins in situ in their natural environment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3160-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Structure of the copper sites in membrane-bound cytochrome c oxidase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.