Ontology highlight
ABSTRACT:
SUBMITTER: Henthorn JT
PROVIDER: S-EPMC6716209 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Henthorn Justin T JT Arias Renee J RJ Koroidov Sergey S Kroll Thomas T Sokaras Dimosthenis D Bergmann Uwe U Rees Douglas C DC DeBeer Serena S
Journal of the American Chemical Society 20190815 34
The size and complexity of Mo-dependent nitrogenase, a multicomponent enzyme capable of reducing dinitrogen to ammonia, have made a detailed understanding of the FeMo cofactor (FeMoco) active site electronic structure an ongoing challenge. Selective substitution of sulfur by selenium in FeMoco affords a unique probe wherein local Fe-Se interactions can be directly interrogated via high-energy resolution fluorescence detected X-ray absorption spectroscopic (HERFD XAS) and extended X-ray absorptio ...[more]