Literature DB >> 6815184

Heat activation of the Fe protein of nitrogenase from Rhodospirillum rubrum.

T E Dowling, G G Preston, P W Ludden.   

Abstract

The Fe protein of nitrogenase from Rhodospirillum rubrum isolated in the inactive form was found to be activated in vitro by heating. This heat activation was dependent upon temperature, pH, and enzyme concentration. During activation by heating, a change in the subunit composition of Fe protein was observed on sodium dodecyl sulfate gels. The upper subunit decreases and the lower subunit increased. All components of the modifying group on inactive Fe protein appear to be lost upon heat activation.

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Year:  1982        PMID： 6815184

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  4 in total

1.  Properties and regulation of glutamine synthetase from Rhodospirillum rubrum.

Authors:  S Nordlund; R H Kanemoto; S A Murrell; P W Ludden
Journal:  J Bacteriol       Date:  1985-01       Impact factor: 3.490

2.  Effect of ammonia, darkness, and phenazine methosulfate on whole-cell nitrogenase activity and Fe protein modification in Rhodospirillum rubrum.

Authors:  R H Kanemoto; P W Ludden
Journal:  J Bacteriol       Date:  1984-05       Impact factor: 3.490

Review 3.  Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes.

Authors:  P W Ludden
Journal:  Mol Cell Biochem       Date:  1994-09       Impact factor: 3.396

4.  Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue.

Authors:  M R Pope; S A Murrell; P W Ludden
Journal:  Proc Natl Acad Sci U S A       Date:  1985-05       Impact factor: 11.205
  4 in total

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