Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Ian Dance"'
Autor:
Ian Dance
Publikováno v:
Dalton Transactions. 52:2013-2026
Promotional N2 (for the HD reaction of nitrogenase) binding at the exo-Fe2 position of FeMo-co allows reducible N2 (forming NH3) to diffuse in and bind exergonically at the endo coordination position of Fe2 or Fe6 in the central reaction domain.
Autor:
Ian Dance
Publikováno v:
Dalton Transactions. 51:15538-15554
Energetically accessible reversible unhooking of S2B or S2BH from Fe2, as an intrinsic property of FeMo-co, needs to be considered in the formulation of mechanisms for the reactions of nitrogenase.
Autor:
Ian Dance
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 51(33)
Additional working hypotheses for the mechanism of the enzyme nitrogenase: the active site uses several binding sites with different mechanistic roles.
Autor:
Ian Dance
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany).
Nitrogenase is the enzyme that converts N
Autor:
Ian Dance
Publikováno v:
Inorganics, Vol 7, Iss 1, p 8 (2019)
The enzyme nitrogenase naturally hydrogenates N2 to NH3, achieved through the accumulation of H atoms on FeMo-co, the Fe7MoS9C(homocitrate) cluster that is the catalytically active site. Four intermediates, E1H1, E2H2, E3H3, and E4H4, carry these hyd
Externí odkaz:
https://doaj.org/article/85dfd74a4db546d99346314452c00704
Autor:
Ian, Dance
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 50(48)
The chemical reactions occurring at the Fe
Autor:
Ian, Dance
Publikováno v:
Journal of inorganic biochemistry. 169
The active site of the enzyme nitrogenase is the FeMo-cofactor (FeMo-co), a C-centred Fe
Autor:
Ian Dance
Publikováno v:
Molecular Simulation. 34:923-929
Publikováno v:
Angewandte Chemie. 114:285-287
Autor:
Ian Dance
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 39(12)
In seeking to mimic the hydrogenation of N(2) to NH(3) as effected under mild conditions by the enzyme nitrogenase, three classes of known metal sulfide clusters that resemble the NFe(7)MoS(9) core of FeMo-co, the active site of nitrogenase, have bee