Linked Life Data

20460724

Source:http://linkedlifedata.com/resource/pubmed/id/20460724

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-5-26
pubmed:abstractText
Homologous cytochromes c(5) from a mesophile, Shewanella amazonensis (SA cytc(5)), and a psychrophile, Shewanella violacea (SV cytc(5)), were compared to elucidate the molecular mechanisms underlying protein stability and function. Cyclic voltammetry revealed that the two proteins had the same redox potential value. Differential scanning calorimetry showed that SV cytc(5) was more stable than SA cytc(5) in an enthalpic manner. These results and the structure model of Shewanella oneidensis cytochrome c(5) indicated that hydrophobic heme environments in the two proteins are the same to maintain the same redox potential value, and that the intra-molecular interactions in SV cytc(5), perhaps involved in Lys-50 and Tyr-73, account for its higher stability. Electron transfer from SV cytc(5) to membrane proteins of S. violacea and S. amazonensis was faster than that from SA cytc(5), suggesting that solvent-exposed Lys-4 in SV cytc(5) is responsible for the faster association and dissociation between SV cytc(5) and its redox partner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1347-6947
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1079-83
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Comparative analysis of highly homologous Shewanella cytochromes c5 for stability and function.
pubmed:affiliation
Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Corporation, Higashi-Hiroshima, Hiroshima, Japan.
pubmed:publicationType
Journal Article, Comparative Study