Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate
نویسندگان
چکیده
منابع مشابه
On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase.
Nitrogenase is activated for N2 reduction by the accumulation of four electrons/protons on its active site FeMo-cofactor, yielding a state, designated as E4, which contains two iron-bridging hydrides [Fe-H-Fe]. A central puzzle of nitrogenase function is an apparently obligatory formation of one H2 per N2 reduced, which would "waste" two reducing equivalents and four ATP. We recently presented ...
متن کاملMisconception of reductive elimination of H2, in the context of the mechanism of nitrogenase.
The elimination of H2 from an M(H)2 component of a coordination complex is often described as reductive elimination, in which the H atoms are regarded as hydride ions, and the product complex after elimination is regarded as reduced by two electrons. The concept is M(n+2)(H(-))2 → M(n) + H2 (with oxidative addition as its reverse). This interpretation contravenes Pauling's electroneutrality pri...
متن کاملEvidence for interstitial carbon in nitrogenase FeMo cofactor.
The identity of the interstitial light atom in the center of the FeMo cofactor of nitrogenase has been enigmatic since its discovery. Atomic-resolution x-ray diffraction data and an electron spin echo envelope modulation (ESEEM) analysis now provide direct evidence that the ligand is a carbon species.
متن کاملActivation and protonation of dinitrogen at the FeMo cofactor of nitrogenase.
The protonation of N2 bound to the active center of nitrogenase has been investigated using state-of-the-art density-functional theory calculations. Dinitrogen in the bridging mode is activated by forming two bonds to Fe sites, which results in a reduction of the energy for the first hydrogen transfer by 123 kJ/mol. The axial binding mode with open sulfur bridge is less reactive by 30 kJ/mol an...
متن کاملStructure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase.
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an α(2)β(2) tetramer that is homologous to the catalytic molybdenum-iron (MoFe) protein (NifDK) component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target locat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Inorganic Chemistry
سال: 2017
ISSN: 0020-1669,1520-510X
DOI: 10.1021/acs.inorgchem.6b02899