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pubmed-article:2784670pubmed:abstractTextThe kinetics of MgATP-induced electron transfer from the Fe protein (Ac2V) to the VFe protein (AclV) of the vanadium-containing nitrogenase from Azotobacter chroococcum were studied by stopped-flow spectrophotometry at 23 degrees C at pH 7.2. They are very similar to those of the molybdenum nitrogenase of Klebsiella pneumoniae [Thorneley (1975) Biochem. J. 145, 391-396]. Extrapolation of the dependence of kobs. on [MgATP] to infinite MgATP concentration gave k = 46 s-1 for the first-order electron-transfer reaction that occurs with the Ac2V MgATPAclV complex. MgATP binds with an apparent KD = 230 +/- 10 microM and MgADP acts as a competitive inhibitor with Ki = 30 +/- 5 microM. The Fe protein and VFe protein associate with k greater than or equal to 3 x 10(7) M-1.s-1. A comparison of the dependences of kobs. for electron transfer on protein concentrations for the vanadium nitrogenase from A. chroococcum with those for the molybdenum nitrogenase from K. pneumoniae [Lowe & Thorneley (1984) Biochem. J. 224, 895-901] indicates that the proteins of the vanadium nitrogenase system form a weaker electron-transfer complex.lld:pubmed
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pubmed-article:2784670pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:2784670pubmed:articleTitleVanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex.lld:pubmed
pubmed-article:2784670pubmed:affiliationA.F.R.C. Institute of Plant Science Research, University of Sussex, Brighton, U.K.lld:pubmed
pubmed-article:2784670pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2784670pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed