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Escherichia coli Flavodoxin

It should be noted that some anaerobic eubacteria (e.g. Escherichia coli, Clostridium acidurici, Chlorobium limicold) possess 2-oxoacid oxidoreductases, either in addition to, or instead of, the dehydrogenase complexes (ref. [37] and references therein). As in the archaebacteria, electrons are transferred to ferredoxin or flavodoxin and the enzymes are small oligomeric proteins. The evolutionary relationships of these enzymes converting pyruvate to acetyl-CoA will be discussed in section 6.2. [Pg.8]

T. F. Havel. Predicting the structure of the flavodoxin from Escherichia coli by homology modeling, distance geometry, and molecular dynamics. Molecular Simulation. 1993, 10, 175—... [Pg.243]

Mclver, L., C. Leadbeater, D.J. Campopiano, R.L. Baxter, S.N. DafF, S.K. Chapman et al. (1998). Characterisation of flavodoxin NADP+ oxido-reductase and flavodoxin key components of electron transfer in Escherichia coli. Em J. Biochem. 257, 577-585. [Pg.148]

Jenkins CM, Waterman MR (1994) Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450C17 hydroxylase activities. J Biol Chem 269 27401-27408... [Pg.397]

Jenkins CM, Waterman MR (1998) NADPH-flavodoxin reductase and flavodoxin from Escherichia coli characteristics as a soluble microsomal P450 reductase. Biochemistry 37 6106-6113... [Pg.397]

Mclver L, Leadbeater C, Campopiano DJ, Baxter RL, Daff SN, Chapman SK, Munro AW (1998) Characterisation of flavodoxin NADP(+) oxidore-ductase and flavodoxin key components of electron transfer in Escherichia coli. Eur J Biochem 257 577-585... [Pg.397]

The recombinant flavorubredoxin from Escherichia coli is an example of a two-component flavoprotein. It consists of a unique arrangement of structural modules in which a large, partly flavodoxin-like domain containing a single FMN is attached to a rubredoxin-like one. In order to assess the role of the rubredoxin domain, Gomes and co-workers have also characterized flavorubredoxin and a truncated form lacking the rubredoxin domain by EPR and optical spectroscopy. Electron donation was found to proceed through the rubredoxin domain of the flavorubredoxin as the rubredoxin truncated protein does not react with flavorubredoxin reductase (the terminal component of the pathway). Thus, it could be concluded that flavorubredoxin is a fusion of a flavoprotein with its redox partner. [Pg.235]


See other pages where Escherichia coli Flavodoxin is mentioned: [Pg.266]    [Pg.652]    [Pg.217]    [Pg.658]    [Pg.154]    [Pg.231]   
See also in sourсe #XX -- [ Pg.740 ]




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