Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1997-8-8
pubmed:databankReference
pubmed:abstractText
Anomalous high viscosity dependence was found in the rate of reaction between the bound cytochrome c and the primary donor bacteriochlorophyll dimer (P840) of the reaction center complex purified from the green sulfur bacterium Chlorobium tepidum. The cytochrome has a primary structure with the N-terminal three membrane-spanning helices connected to the extended C-terminal heme-containing hydrophilic moiety. The rate constant of the reaction decreased from 5.0 x 10(3) s-1 to 1.0 x 10 s-1 as the glycerol concentration increased from 0 to 60% (v/v) at 295 K, showing a linear dependence on the -2.4th power of the specific viscosity. The glycerol effect was fully reversible. The extraordinary high viscosity dependence cannot be explained by the simple diffusive Brownian fluctuation model and suggests that the electron transfer mechanism is dependent on the unique conformational fluctuations of the heme-containing moiety of cytochrome c.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9267-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Viscosity dependence of the electron transfer rate from bound cytochrome c to P840 in the photosynthetic reaction center of the green sulfur bacterium Chlorobium tepidum.
pubmed:affiliation
Department of Biology, Graduate School of Science, Osaka University, Osaka 560, Japan. ohoka@bio.sci.osaka-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't