pubmed-article:2784670 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2784670 | lifeskim:mentions | umls-concept:C0995322 | lld:lifeskim |
pubmed-article:2784670 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
pubmed-article:2784670 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
pubmed-article:2784670 | lifeskim:mentions | umls-concept:C0042307 | lld:lifeskim |
pubmed-article:2784670 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:2784670 | pubmed:dateCreated | 1989-4-25 | lld:pubmed |
pubmed-article:2784670 | pubmed:abstractText | The 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:2784670 | pubmed:language | eng | lld:pubmed |
pubmed-article:2784670 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2784670 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2784670 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2784670 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2784670 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2784670 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2784670 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2784670 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2784670 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:2784670 | pubmed:author | pubmed-author:EadyR RRR | lld:pubmed |
pubmed-article:2784670 | pubmed:author | pubmed-author:OWENNN | lld:pubmed |
pubmed-article:2784670 | pubmed:author | pubmed-author:ThorneleyR... | lld:pubmed |
pubmed-article:2784670 | pubmed:author | pubmed-author:BergströmN... | lld:pubmed |
pubmed-article:2784670 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2784670 | pubmed:day | 1 | lld:pubmed |
pubmed-article:2784670 | pubmed:volume | 257 | lld:pubmed |
pubmed-article:2784670 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2784670 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2784670 | pubmed:pagination | 789-94 | lld:pubmed |
pubmed-article:2784670 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:2784670 | pubmed:meshHeading | pubmed-meshheading:2784670-... | lld:pubmed |
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pubmed-article:2784670 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2784670 | pubmed:articleTitle | Vanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex. | lld:pubmed |
pubmed-article:2784670 | pubmed:affiliation | A.F.R.C. Institute of Plant Science Research, University of Sussex, Brighton, U.K. | lld:pubmed |
pubmed-article:2784670 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2784670 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |