Linked Life Data

2163273

Source:http://linkedlifedata.com/resource/pubmed/id/2163273

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1990-8-6
pubmed:abstractText
Resonance Raman spectra of Chromatium vinosum cytochrome c' have been obtained for the five pH-dependent states of the protein [i.e., types I (pH 7), II (pH 10), and III (pH 12) of the ferric protein and type a (pH 7) and type n (pH 12) of the ferrous protein]. The raman spectra of type II and type a are consistent with those of high-spin, 5-coordinate heme proteins, such as deoxyhemoglobin, while spectra of type III and type n correspond more closely to those of low-spin, ferric and ferrous cytochrome c, respectively. Spectra of the CO-bound equilibrium species qualitatively resemble those of carbon monoxy human HbA. However, both the Fe-C and C = O stretching modes of the ligated species exhibit pH-dependent frequency shifts. Our data also indicate that CO photolysis is much more efficient at pH 7 than at pH 12. Moreover, the spectra of the photolytic transients suggest that unique, high-spin species are formed subsequent to CO photolysis from both type a and type n species.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4166-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Resonance Raman characterization of Chromatium vinosum cytochrome c'. Effect of pH and comparison of equilibrium and photolyzed carbon monoxide species.
pubmed:affiliation
Department of Chemistry, University of New Mexico, Albuquerque 87131.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.