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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1989-4-25
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-1098654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-173545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-180978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-2821997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-2833236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-2851977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3021770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3026449,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3140782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3162672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3164616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3318808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3322266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-336036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3474027,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-363454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-3890886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-6316927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-6395861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-6395863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-6395864,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-648533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2784670-6982070
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
257
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
789-94
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1989
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pubmed:articleTitle |
Vanadium nitrogenase of Azotobacter chroococcum. MgATP-dependent electron transfer within the protein complex.
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pubmed:affiliation |
A.F.R.C. Institute of Plant Science Research, University of Sussex, Brighton, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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