1995
DOI: 10.1074/jbc.270.36.21258
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Azotobacter vinelandii NADPH:Ferredoxin Reductase Cloning, Sequencing, and Overexpression

Abstract: Azotobacter vinelandii ferredoxin I (AvFdI) controls the expression of another protein that was originally designated Protein X. Recently we reported that Protein X is a NADPH-specific flavoprotein that binds specifically to FdI (Isas, J. M., and Burgess, B. K. (1994) J. Biol. Chem. 269, 19404 -19409). The gene encoding this protein has now been cloned and sequenced. Protein X is 33% identical and has an overall 53% similarity with the fpr gene product from Escherichia coli that encodes NADPH:ferredoxin reduct… Show more

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Cited by 33 publications
(42 citation statements)
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“…The first includes the plant-type FNRs that are monomeric enzymes also found in eukaryotic algae as well as in cyanobacteria, and have been intensively reviewed (Arakaki et al 1997). The second group is sometimes called the bacteria type and is composed of monomeric FNRs from some bacteria such as Escherichia coli (Bianchi et al 1993) and Azotobacter vinelandii (Isas et al 1995). There are significant similarities between these two groups of FNRs in 3-D structure (Prasad et al 1998) as well as in amino acid sequence (Arakaki et al 1997, Ceccarelli et al 2004).…”
Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning
confidence: 99%
“…The first includes the plant-type FNRs that are monomeric enzymes also found in eukaryotic algae as well as in cyanobacteria, and have been intensively reviewed (Arakaki et al 1997). The second group is sometimes called the bacteria type and is composed of monomeric FNRs from some bacteria such as Escherichia coli (Bianchi et al 1993) and Azotobacter vinelandii (Isas et al 1995). There are significant similarities between these two groups of FNRs in 3-D structure (Prasad et al 1998) as well as in amino acid sequence (Arakaki et al 1997, Ceccarelli et al 2004).…”
Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning
confidence: 99%
“…In order to investigate the mechanism of regulation by FdI, the small acidic protein that is overexpressed in response to fdxA deletion was purified and characterized (15), and the gene encoding the protein was cloned and sequenced (16). The protein was shown to be a M r ϳ29,000 NADPH-ferredoxin reductase that was designated FPR because its physical properties and amino acid sequence showed striking similarity to the FPR from Escherichia coli (15,17,18).…”
Section: Azotobacter Vinelandii Ferredoxin I (Avfdi)mentioning
confidence: 99%
“…In order to investigate the mechanism of regulation by FdI, the small acidic protein that is overexpressed in response to fdxA deletion was purified and characterized (15), and the gene encoding the protein was cloned and sequenced (16). The protein was shown to be a M r ϳ29,000 NADPH-ferredoxin reductase that was designated FPR because its physical properties and amino acid sequence showed striking similarity to the FPR from Escherichia coli (15,17,18). In E. coli, the protein appears to be part of a system that activates at least three different enzymes involved in anaerobic metabolism: anaerobic ribonucleotide reductase (19), pyruvate formate-lyase (20), and cobalamin-dependent methionine synthase (21).…”
Section: Azotobacter Vinelandii Ferredoxin I (Avfdi)mentioning
confidence: 99%
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“…This type of FNR transfers reducing equivalents from the photo-reduced [2Fe-2S] Fd to NADP + , providing the NADPH needed for CO 2 assimilation and other metabolic pathways (Karplus & Faber, 2004). Bacterial-type FNRs utilize NAD(P)H in order to reduce Fd and/or flavodoxin (Isas & Burgess, 1994;Liochev et al, 1994). The physiological electron flow catalyzed by this type of FNR is the converse of that of chloroplast-type FNRs.…”
Section: Introductionmentioning
confidence: 99%