Linked Life Data

12516783

Source:http://linkedlifedata.com/resource/pubmed/id/12516783

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2003-1-8
pubmed:abstractText
The single cysteine in the b subunit of the membranous F0 sector and the 19 cysteines in extramembranous F1 sector of the Escherichia coli ATP synthase were replaced by alanine. When cells were grown under anaerobic conditions on glucose, the kcat for ATP hydrolysis of membrane vesicles containing the bCys21Ala mutant enzyme, but not enzymes with other cysteine replacements, was lower, while ATP-driven H+ pumping was unchanged. However, the ATP-dependent increase in the number of accessible thiol groups in membrane vesicles was negated. Furthermore, K+ uptake and molecular hydrogen production by whole cells and protoplasts was greatly decreased. These results indicate a role for the F0 subunit bCys21 in the functionality of F0F1 and coupling to other membranous activities under fermentative conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0144-8463
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-30
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:articleTitle
F0 cysteine, bCys21, in the Escherichia coli ATP synthase is involved in regulation of potassium uptake and molecular hydrogen production in anaerobic conditions.
pubmed:affiliation
Department of Biophysics, Yerevan State University, 1 Alex Manougian Street, 375049 Yerevan, Armenia.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't