Ontology highlight
ABSTRACT:
SUBMITTER: Tabrizi SG
PROVIDER: S-EPMC4819768 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Tabrizi Shadan Ghassemi SG Pelmenschikov Vladimir V Noodleman Louis L Kaupp Martin M
Journal of chemical theory and computation 20151216 1
An unprecedented [4Fe-3S] cluster proximal to the regular [NiFe] active site has recently been found to be responsible for the ability of membrane-bound hydrogenases (MBHs) to oxidize dihydrogen in the presence of ambient levels of oxygen. Starting from proximal cluster models of a recent DFT study on the redox-dependent structural transformation of the [4Fe-3S] cluster, (57)Fe Mössbauer parameters (electric field gradients, isomer shifts, and nuclear hyperfine couplings) were calculated using D ...[more]