Linked Life Data

2765533

Source:http://linkedlifedata.com/resource/pubmed/id/2765533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1989-10-6
pubmed:abstractText
The NMR spectra of the high-potential iron protein from the photosynthetic bacterium Chromatium gracile and its ruthenium-labeled (His-42 and His-20) derivatives are reported. The isotropically shifted resonances in both the oxidized and reduced forms show a complex pH dependence due to the presence of three ionizable residues (Glu-44, His-20, and His-42). Assignments have been made to specific residues and the spectral features compared to those of other bacterial HiPIP's. The decrease in the reduction potential with increasing pH for this class of proteins is attributed to stabilization of the oxidized state of the cluster by delocalization of electron density onto the neighboring Tyr-19 residue.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5261-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
1H NMR characterization of Chromatium gracile high-potential iron protein and its ruthenium-modified derivatives. Modulation of the reduction potentials in low- and high-potential [Fe4S4] ferredoxins.
pubmed:affiliation
Arthur Amos Noyes Laboratory, 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