Evidence on the role(s) of atp in the mechanism of nitrogenase, from proton nmr relaxation studies on metal and nucleotide binding to the molybdenum-iron protein
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference32 articles.
1. Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae
2. Mössbauer spectroscopy of the nitrogenase proteins from Klebsiella pneumoniae. Structural assignments and mechanistic conclusions
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1. Biosynthesis of the Iron-Molydbenum and Iron-Vanadium Cofactors of the nif- and vnf-Encoded Nitrogenases;Catalysts for Nitrogen Fixation;2004
2. Covalent modification of nitrogenase MoFe protein by ADP;Biochemical Journal;1997-03-15
3. Isolation and characterization of nitrogenase MoFe protein from the mutant strain pHK17 of Klebsiella pneumoniae in which the two bridging cysteine residues of the P-clusters are replaced by the non-coordinating amino acid alanine;Biochemical Journal;1996-08-15
4. Energy transduction by nitrogenase: binding of MgADP to the MoFe protein is dependent on the oxidation state of the iron-sulphur ‘P’ clusters;Biochemical Journal;1993-05-01
5. Reactivities and biological functions of iron-sulfur clusters;Journal of Cluster Science;1990-03
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