Vanadium (V) is reduced by the 'as isolated' nitrogenase Fe-protein at neutral pH |
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Authors: | Fisher Karl Lowe David J Petersen Jan |
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Institution: | Department of Biological Chemistry, John Innes Centre, Colney Lane, Norwich, UK. |
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Abstract: | 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. |
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