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- Shen, J.; Dean, D.R.; Newton, W.E.
- Biochemistry 1997 v.36 no.16 pp. 4884-4894
- Azotobacter vinelandii; binding sites; catalytic activity; electron paramagnetic resonance spectroscopy; hydrogen cyanide; mutants; nitrogen fixation; nitrogenase; phenotype; polypeptides; protons
- ... The arginine-277 residue of the alpha-subunit of the nitrogenase MoFe protein was targeted for substitution because it is (i) a close neighbor of alpha-cysteine-275, which is one of only two residues anchoring the FeMo cofactor to the polypeptide, and (ii) a component of a potential channel for entry/exit of substrates/ products and for accepting FeMo cofactor during MoFe-protein maturation. Sever ...
- Kahn, K.; Tipton, P.A.
- Biochemistry 1997 v.36 no.16 pp. 4731-4738
- Escherichia coli; absorbance; argon (noble gases); copper; enzymatic reactions; genes; ionization; matrix-assisted laser desorption-ionization mass spectrometry; models; molecular weight; monitoring; oxygen; pH; root nodules; soybeans; xanthine
- ... The kinetic mechanism of urate oxidase isolated from soybean root nodules has been determined by initial velocity kinetic studies monitoring oxygen uptake, in order to avoid potential artifacts in the spectrophotometric assay which arise from absorbance due to unidentified products of the enzymatic reaction. Urate and O2 bind to the enzyme sequentially; xanthine is a competitive inhibitor versus u ...