dc.contributor.author
Laun, Konstantin
dc.contributor.author
Mebs, Stefan
dc.contributor.author
Duan, Jifu
dc.contributor.author
Wittkamp, Florian
dc.contributor.author
Apfel, Ulf-Peter
dc.contributor.author
Happe, Thomas
dc.contributor.author
Winkler, Martin
dc.contributor.author
Haumann, Michael
dc.contributor.author
Stripp, Sven T.
dc.date.accessioned
2018-08-21T04:27:47Z
dc.date.available
2018-08-21T04:27:47Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/22746
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-544
dc.description.abstract
[FeFe]-hydrogenases efficiently catalyzes hydrogen conversion at a unique [4Fe–4S]-[FeFe] cofactor, the so-called H-cluster. The catalytic reaction occurs at the diiron site, while the [4Fe–4S] cluster functions as a redox shuttle. In the oxidized resting state (Hox), the iron ions of the diiron site bind one cyanide (CN−) and carbon monoxide (CO) ligand each and a third carbonyl can be found in the Fe–Fe bridging position (µCO). In the presence of exogenous CO, A fourth CO ligand binds at the diiron site to form the oxidized, CO-inhibited H-cluster (Hox-CO). We investigated the reduced, CO-inhibited H-cluster (Hred´-CO) in this work. The stretching vibrations of the diatomic ligands were monitored by attenuated total reflection Fourier-transform infrared spectroscopy (ATR FTIR). Density functional theory (DFT) at the TPSSh/TZVP level was employed to analyze the cofactor geometry, as well as the redox and protonation state of the H-cluster. Selective 13CO isotope editing, spectro-electrochemistry, and correlation analysis of IR data identified a one-electron reduced, protonated [4Fe–4S] cluster and an apical CN− ligand at the diiron site in Hred´-CO. The reduced, CO-inhibited H-cluster forms independently of the sequence of CO binding and cofactor reduction, which implies that the ligand rearrangement at the diiron site upon CO inhibition is independent of the redox and protonation state of the [4Fe–4S] cluster. The relation of coordination dynamics to cofactor redox and protonation changes in hydrogen conversion catalysis and inhibition is discussed.
en
dc.format.extent
13 Seiten
de
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
de
dc.subject
metalloenzymes
en
dc.subject
FTIR spectro-electrochemistry
en
dc.subject
hydrogenases
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik::530 Physik
de
dc.title
Spectroscopical Investigations on the Redox Chemistry of [FeFe]-Hydrogenases in the Presence of Carbon Monoxide
de
dc.type
Wissenschaftlicher Artikel
de
dcterms.bibliographicCitation.articlenumber
1669
dcterms.bibliographicCitation.doi
10.3390/molecules23071669
dcterms.bibliographicCitation.journaltitle
Molecules
dcterms.bibliographicCitation.number
7
dcterms.bibliographicCitation.volume
23
dcterms.bibliographicCitation.url
https://doi.org/10.3390/molecules23071669
de
refubium.affiliation
Physik
de
refubium.funding
Institutional Participation
de
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin und der DFG gefördert.
de
refubium.resourceType.isindependentpub
no
de
dcterms.accessRights.dnb
free
de
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1420-3049