Vanadium (V) is reduced by the 'as isolated' nitrogenase Fe-protein at neutral pH.
Orthovanadate has been investigated in the presence of the nitrogenase Fe-protein. Electron paramagnetic resonance (EPR) spectra demonstrate that vanadium (V) is reduced by the reduced Fe-protein to vanadium (IV) which then probably binds to the nucleotide binding site in place of the Mg2+ which is normally present. In contrast, the oxidized Fe-protein is unable to reduce vanadate. In this case vanadate has potential for use as a phosphate analogue where it acts as transition state mimic for hydrolysis.
Fisher
Karl
K
Department of Biological Chemistry, John Innes Centre, Colney Lane, Norwich, UK.
Lowe
David J
DJ
Petersen
Jan
J
D016948:Azotobacter vinelandii / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000737:chemistry* / Q000378:metabolism*; D009591:Nitrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D014639:Vanadium / Q000737:chemistry* / Q000378:metabolism*
D014639:Vanadium; D007501:Iron; D009591:Nitrogenase