Ontology highlight
ABSTRACT:
SUBMITTER: Gu NX
PROVIDER: S-EPMC6592702 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20180510 20
Believed to accumulate on the Fe sites of the FeMo-cofactor (FeMoco) of MoFe-nitrogenase under turnover, strongly donating hydrides have been proposed to facilitate N<sub>2</sub> binding to Fe and may also participate in the hydrogen evolution process concomitant to nitrogen fixation. Here, we report the synthesis and characterization of a thiolate-coordinated Fe<sup>III</sup>(H)(N<sub>2</sub>) complex, which releases H<sub>2</sub> upon warming to yield an Fe<sup>II</sup>-N<sub>2</sub>-Fe<sup>II ...[more]