Linked Life Data

3027081

Source:http://linkedlifedata.com/resource/pubmed/id/3027081

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-3-4
pubmed:abstractText
Resonance Raman and electron paramagnetic resonance spectroscopy have been utilized to identify histidine as an axial heme ligand in a high spin, heme c-containing protein isolated from the photosynthetic purple sulfur bacterium Chromatium vinosum. Resonance Raman spectroscopy has also been used to characterize the CO adduct of the C. vinosum hemoprotein. Resonance Raman spectra of the heme site obtained within 10 ns of CO photolysis from the ferrous hemoprotein are virtually identical to those of the unligated protein, indicating that there is little or no rearrangement of the heme pocket in response to ligand photolysis. The equilibrium constant for CO binding to the ferrous hemeprotein was measured to be 1.7 X 10(-5) M-1 and the CO association rate constant determined to be 5.4 X 10(3) M-1 S-1. The quantum efficiency for photodissociation of the hemoprotein X CO complex was greater than or equal to 0.9.
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
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1144-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Spectroscopic and kinetic properties of an oxygen-binding heme protein from Chromatium vinosum.
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