Regulation of the F0F1-ATP synthase: The conformation of subunit epsilon might be determined by directionality of subunit gamma rotation

DC FieldValueLanguage
dc.contributor.authorFeniouk, BA
dc.contributor.authorJunge, W
dc.date.accessioned2021-12-23T16:13:32Z-
dc.date.available2021-12-23T16:13:32Z-
dc.date.issued2005
dc.identifier.issn18733468
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10616-
dc.description.abstractF0F1-ATP synthase couples ATP synthesis/hydrolysis with transmembrane proton transport. The catalytic mechanism involves rotation of the gamma epsilon(similar to 10)-subunits complex relative to the rest of the enzyme. In the absence of protonmotive force the enzyme is inactivated by the tight binding of MgADP. Subunit F also modulates the activity: its conformation can change from a contracted to extended form with C-terminus stretched towards F-1. The latter form ihnibits ATP hydrolysis (but not synthesis). We propose that the directionality of the coiled-coil subunit gamma rotation determines whether subunit E is in contracted or extended form. Block of rotation by MgADP presumably induces the extended conformation of subunit F. This conformation might serve as a safety lock, stabilizing the ADP-inhibited state upon de-energization and preventing spontaneous re-activation and wasteful ATP hydrolysis. The hypothesis merges the known regulatory effects of ADP, protonmotive force and conformational changes of subunit epsilon into a consistent picture. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofFEBS LETTERS
dc.subjectactivation
dc.subjectADP inhibition
dc.subjectALPHA(3)BETA(3)GAMMA COMPLEX
dc.subjectATP synthase
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCATALYTIC SITE
dc.subjectCell Biology
dc.subjectCHLOROPLAST ATP SYNTHASE
dc.subjectENERGY-DEPENDENT TRANSFORMATION
dc.subjectESCHERICHIA-COLI F1-ATPASE
dc.subjectMITOCHONDRIAL F1-ATPASE
dc.subjectNONCATALYTIC SITES
dc.subjectPROTON MOTIVE FORCE
dc.subjectprotonmotive force
dc.subjectregulation
dc.subjectsubunit epsilon
dc.subjectTHERMOPHILIC BACILLUS PS3
dc.subjectTIGHTLY BOUND ADP
dc.titleRegulation of the F0F1-ATP synthase: The conformation of subunit epsilon might be determined by directionality of subunit gamma rotation
dc.typejournal article
dc.identifier.doi10.1016/j.febslet.2005.08.030
dc.identifier.isiISI:000232194300002
dc.description.volume579
dc.description.issue23
dc.description.startpage5114
dc.description.endpage5118
dc.contributor.orcid0000-0003-0474-7411
dc.contributor.researcheridF-2380-2012
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationFEBS Lett.
dcterms.oaStatusBronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidJuWo587-
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