Rotatory catalysis by F-ATPase: Real-time recording of intersubunit rotation

DC FieldValueLanguage
dc.contributor.authorJunge, W
dc.contributor.authorSabbert, D
dc.contributor.authorEngelbrecht, S
dc.date.accessioned2021-12-23T15:57:17Z-
dc.date.available2021-12-23T15:57:17Z-
dc.date.issued1996
dc.identifier.issn00059021
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/2827-
dc.description95th Annual Meeting of the Deutsche-Bunsen-Gesellschaft-fur-Physikalische-Chemie on Primary Processes of Photosynthesis, JENA, GERMANY, MAY 16-18, 1996
dc.description.abstractATP synthase (F-ATPase) is an ubiquitous enzyme in photosynthesis and respiration of prokaryotic and eukaryotic organisms. It couples proton translocation through its membrane portion, F-0, to the synthesis of the `'energy carrier molecule'' ATP at the peripheral portion, F-1 [1]. Three cooperative reaction sites are distributed with trigonal symmetry over the hexagonal array of (alpha beta)(3) in F-1 [2, 3]. It has been proposed that the endergonic release of spontaneously formed ATP [4, 5] might involve mechanical energy transduction [6, 7] through the proton driven rotation of subunit gamma within (alpha beta)(3) [2, 8, 9]. We recorded the putative intersubunit rotation in real rime [10]. Applying polarized absorption relaxation after photobleaching (PARAP) to immobilized F-1 with eosinlabeled gamma, we observed the rotational motion of gamma relative to immobilized (alpha beta)(3) in the time range of 100 ms, compatible with the rate of ATP hydrolysis by immobilized F-1. Its angular domain of at least 200 degrees favours a rotatory tri-site mechanism of catalysis with gamma acting as a crankshaft in the center of (alpha beta)(3).
dc.language.isoen
dc.publisherVCH PUBLISHERS INC
dc.relation.ispartofBERICHTE DER BUNSEN-GESELLSCHAFT-PHYSICAL CHEMISTRY CHEMICAL PHYSICS
dc.subjectBACTERIAL FLAGELLAR MOTOR
dc.subjectBINDING
dc.subjectbiophysical chemistry
dc.subjectcatalysis
dc.subjectChemistry
dc.subjectChemistry, Physical
dc.subjectDELTA
dc.subjectdiffusion
dc.subjectESCHERICHIA-COLI F1-ATPASE
dc.subjectFLUORESCENCE
dc.subjectGAMMA-SUBUNIT
dc.subjectMECHANISM
dc.subjectmolecular structure
dc.subjectprotein dynamics (molecular dynamics)
dc.subjectSITES
dc.subjectSYNTHASE
dc.titleRotatory catalysis by F-ATPase: Real-time recording of intersubunit rotation
dc.typeconference paper
dc.identifier.doi10.1002/bbpc.19961001215
dc.identifier.isiISI:A1996WB83300014
dc.description.volume100
dc.description.issue12
dc.description.startpage2014
dc.description.endpage2019
dc.publisher.place303 NW 12TH AVE, DEERFIELD BEACH, FL 33442-1788
dcterms.isPartOf.abbreviationBer. Bunsen-Ges. Phys. Chem. Chem. Phys.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidJuWo587-
Show simple item record

Page view(s)

2
Last Week
0
Last month
0
checked on Apr 15, 2024

Google ScholarTM

Check

Altmetric