Nitrogenase and homologs
نویسندگان
چکیده
منابع مشابه
Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
UNLABELLED The L-cluster is an all-iron homolog of nitrogenase cofactors. Driven by europium(II) diethylenetriaminepentaacetate [Eu(II)-DTPA], the isolated L-cluster is capable of ATP-independent reduction of CO and CN(-) to C1 to C4 and C1 to C6 hydrocarbons, respectively. Compared to its cofactor homologs, the L-cluster generates considerably more CH4 from the reduction of CO and CN(-), which...
متن کاملIdentification and characterization of functional homologs of nitrogenase cofactor biosynthesis protein NifB from methanogens.
Nitrogenase biosynthesis protein NifB catalyzes the radical S-adenosyl-L-methionine (SAM)-dependent insertion of carbide into the M cluster, the cofactor of the molybdenum nitrogenase from Azotobacter vinelandii. Here, we report the identification and characterization of two naturally "truncated" homologs of NifB from Methanosarcina acetivorans (NifB(Ma)) and Methanobacterium thermoautotrophicu...
متن کاملNitrogenase Complex
The nitrogenase complex carries out the fixation of nitrogen by reducing molecular dinitrogen (N2) to ammonium (NH4 1 ) and also reduces acetylene to ethylene. The two component proteins are dinitrogenase and dinitrogenase reductase. Although different metals can form the metal clusters contained in nitrogenase proteins, all nitrogenases have similar properties. The nitrogenase enzyme system is...
متن کاملElectron paramagnetic resonance of nitrogenase and nitrogenase components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP.
The electron paramagnetic resonance of nitrogenase components, separately and together with the other reactants in the nitrogenase system (namely, reductant and Mg.ATP), have been examined at low temperatures (<20 degrees K). The MoFe protein, component I or molybdoferredoxin, in the oxidized (but not oxygen-inactivated) state yields signals with g-values of 4.3, 3.7, and 2.01, and when reduced...
متن کاملFeedback inhibition of nitrogenase.
No inhibition of nitrogenase activity by physiological levels of NH4+ or carbamyl phosphate was observed in extracts of Azotobacter vinelandii. All of the 15N2 reduced by cultures which received no NH4+ was found in the cells. By contrast, more than 95% of the 15N2 reduced by cultures which had been given NH4+ was found in the medium. Failure to examine the culture medium would lead to the erro...
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: JBIC Journal of Biological Inorganic Chemistry
سال: 2014
ISSN: 0949-8257,1432-1327
DOI: 10.1007/s00775-014-1225-3