QM/MM Study of Partial Dissociation of S2B for the E2 Intermediate of Nitrogenase
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DOI: 10.1021/acs.inorgchem.2c02488
Abstract: Nitrogenase is the only enzyme that can cleave the triple bond in N2, making nitrogen available for all lifeforms. Previous computational studies have given widely diverging results regarding the reaction mechanism of the enzyme. For… read more here.
Keywords: s2b; study partial; nitrogenase; s2b intermediate ... See more keywords
Understanding the tethered unhooking and rehooking of S2B in the reaction domain of FeMo-co, the active site of nitrogenase.
Sign Up to like & getrecommendations! Published in 2022 at "Dalton transactions"
DOI: 10.1039/d2dt02571j
Abstract: The active site of the nitrogen fixing enzyme nitrogenase is an Fe7MoS9C cluster, and investigations of the enigmatic chemical mechanism of the enzyme have focussed on a pair of Fe atoms, Fe2 and Fe6, and… read more here.
Keywords: s2b; tethered unhooking; nitrogenase; unhooking s2b ... See more keywords