Fe−Mo system
نویسندگان
چکیده
منابع مشابه
FeMo cofactor maturation on NifEN.
FeMo cofactor (FeMoco) biosynthesis is one of the most complicated processes in metalloprotein biochemistry. Here we show that Mo and homocitrate are incorporated into the Fe/S core of the FeMoco precursor while it is bound to NifEN and that the resulting fully complemented, FeMoco-like cluster is transformed into a mature FeMoco upon transfer from NifEN to MoFe protein through direct protein-p...
متن کاملDiversity and Functional Analysis of the FeMo-Cofactor Maturase NifB
One of the main hurdles to engineer nitrogenase in a non-diazotrophic host is achieving NifB activity. NifB is an extremely unstable and oxygen sensitive protein that catalyzes a low-potential SAM-radical dependent reaction. The product of NifB activity is called NifB-co, a complex [8Fe-9S-C] cluster that serves as obligate intermediate in the biosyntheses of the active-site cofactors of all kn...
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 کاملNitrogenase consists of two proteins: an iron containing protein and an iron and molybdenum (FeMo) containing protedl,21. Recent analyses[3] of MO EXAFS data of the FeMo protein and the FeMo
Nitrogenase consists of two proteins: an iron containing protein and an iron and molybdenum (FeMo) containing protedl,21. Recent analyses[3] of MO EXAFS data of the FeMo protein and the FeMo COfactod41 isolated from it have led to the conclusion that the Mo atom is prinprily coordinated to sulfur and is separated by < 3 A from another metal atom, not Mo and,therefore, Fe, and that the Mo coordi...
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...
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ژورنال
عنوان ژورنال: Bulletin of Alloy Phase Diagrams
سال: 1983
ISSN: 0197-0216
DOI: 10.1007/bf02880313