Linked Life Data

8382524

Source:http://linkedlifedata.com/resource/pubmed/id/8382524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1993-3-29
pubmed:abstractText
The interactions of azide and thiocyanate with the binuclear center of oxidized cytochrome c oxidase have been characterized by Fourier transform infrared and UV-vis spectroscopy, electron paramagnetic resonance and magnetic and natural circular dichroism. Azide binds in two phases, a high-affinity phase (Kd = 64 microM) in which it is bound as a bridge to the binuclear center and a low-affinity phase (Kd = 20 mM) in which it displaces one of the axial ligands to cytochrome a. Thiocyanate also binds in two phases. The high-affinity phase (Kd = 2.7 mM) involves binding in a terminal mode to CuB; the low-affinity phase is complex and involves both CuA and cytochrome a. In contrast to the recent proposal of Yoshikawa and Caughey [(1990) J. Biol. Chem. 265, 7945-7958], we conclude that cyanide also functions as a bridge between cytochrome a3 and CuB. In the presence of cyanide, azide does not bind to its high-affinity site but thiocyanate does bind to its high-affinity site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1833-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Spectroscopic characterization of the interaction of azide and thiocyanate with the binuclear center of cytochrome oxidase: evidence for multiple ligand sites.
pubmed:affiliation
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251-1892.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't