dc.contributor.author
Schrapers, Peer
dc.contributor.author
Ilina, Julia
dc.contributor.author
Gregg, Christina M.
dc.contributor.author
Mebs, Stefan
dc.contributor.author
Jeoung, Jae-Hun
dc.contributor.author
Dau, Holger
dc.contributor.author
Dobbek, Holger
dc.contributor.author
Haumann, Michael
dc.date.accessioned
2018-06-08T10:24:37Z
dc.date.available
2017-07-24T12:53:42.808Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/20384
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-23687
dc.description.abstract
Bacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the
Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a
[4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with
proximal, p, and distal, d, ions) was studied by X-ray absorption spectroscopy
in ACS variants comprising all three protein domains or only the C-terminal
domain with the A-cluster. Both variants showed two square-planar Ni(II) sites
and an OH- bound at Ni(II)p in oxidized enzyme and a H2O at Ni(I)p in reduced
enzyme; a Ni(I)p-CO species was induced by CO incubation and a Ni(II)-CH3-
species with an additional water ligand by a methyl group donor. These
findings render a direct effect of the N-terminal and middle domains on the
A-cluster structure unlikely.
en
dc.format.extent
14 Seiten
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik::530 Physik
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie
dc.title
Ligand binding at the A-cluster in full-length or truncated acetyl-CoA
synthase studied by Xray absorption spectroscopy
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
PLoS ONE 12(2): e0171039
dcterms.bibliographicCitation.doi
10.1371/journal.pone.0171039
dcterms.bibliographicCitation.url
http://doi.org/doi:10.1371/journal.pone.0171039
refubium.affiliation
Physik
de
refubium.funding
Deutsche Forschungsgemeinschaft (DFG)
refubium.mycore.fudocsId
FUDOCS_document_000000027226
refubium.note.author
Gefördert durch die DFG und den Open-Access-Publikationsfonds der Freien
Universität Berlin.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000008352
dcterms.accessRights.openaire
open access