Constant c(10) Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking

DC ElementWertSprache
dc.contributor.authorBallhausen, Britta
dc.contributor.authorAltendorf, Karlheinz
dc.contributor.authorDeckers-Hebestreit, Gabriele
dc.date.accessioned2021-12-23T16:03:16Z-
dc.date.available2021-12-23T16:03:16Z-
dc.date.issued2009
dc.identifier.issn00219193
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/5894-
dc.description.abstractThe subunit c stoichiometry of Escherichia coli ATP synthase was studied by intermolecular cross-linking via oxidation of bi-cysteine-substituted subunit c (cA21C/cM65C). Independent of the carbon source used for growth and independent of the presence of other F0F1 subunits, an equal pattern of cross-link formation stopping at the formation of decamers was obtained.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 431/P2]; We thank Brigitte Herkenhoff-Hesselmann for familiarizing Britta Ballhausen with the technical details necessary to perform these experiments, Heiner Brookman for generating E. coli strain HB1(DE3), and Jorg-Christian Greie for critical reading of the manuscript.; This work was supported by a grant from the Deutsche Forschungsgemeinschaft (SFB 431/P2).
dc.language.isoen
dc.publisherAMER SOC MICROBIOLOGY
dc.relation.ispartofJOURNAL OF BACTERIOLOGY
dc.subjectEXPRESSION
dc.subjectF-0 SECTOR
dc.subjectF1F0 ATPASE
dc.subjectGENES
dc.subjectH+/ATP RATIO
dc.subjectMEMBRANE
dc.subjectMicrobiology
dc.subjectMODEL
dc.subjectPROTON-TRANSLOCATING ATPASE
dc.subjectROTOR RING
dc.subjectSUBUNIT C OLIGOMER
dc.titleConstant c(10) Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking
dc.typejournal article
dc.identifier.doi10.1128/JB.01390-08
dc.identifier.isiISI:000264085500047
dc.description.volume191
dc.description.issue7
dc.description.startpage2400
dc.description.endpage2404
dc.publisher.place1752 N ST NW, WASHINGTON, DC 20036-2904 USA
dcterms.isPartOf.abbreviationJ. Bacteriol.
dcterms.oaStatusGreen Published, Bronze, Green Submitted
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidAlKa770-
crisitem.author.netidDeGa700-
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