PMID:8292013: Difference between revisions

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<span style = 'font-size: large'> '''Eschenbrenner, M, Coves, J and Fontecave, M'''  (1994) Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein.''Biochem. Biophys. Res. Commun.'' '''198''':127-31</span>
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!align=left  |Citation
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'''Eschenbrenner, M, Coves, J and Fontecave, M'''  (1994) Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein. ''Biochem. Biophys. Res. Commun.'' '''198''':127-31
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!align=left  |Abstract
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The haemoglobin-like protein (HMP) of E. coli previously isolated as a dihydropteridine reductase was shown to be also a ferric citrate reductase. We demonstrate that, in fact, HMP is a flavin reductase and that its ferric reductase activity is a result of its ability to reduce free flavins. However, when compared to the two main ferric/flavin reductases of E. coli, i.e., the NAD(P)H: flavin oxidoreductase and the sulfite reductase, one can conclude that the contribution of HMP to iron reduction is negligible.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8292013 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The haemoglobin-like protein (HMP) of E. coli previously isolated as a dihydropteridine reductase was shown to be also a ferric citrate reductase. We demonstrate that, in fact, HMP is a flavin reductase and that its ferric reductase activity is a result of its ability to reduce free flavins. However, when compared to the two main ferric/flavin reductases of E. coli, i.e., the NAD(P)H: flavin oxidoreductase and the sulfite reductase, one can conclude that the contribution of HMP to iron reduction is negligible.
!align=left  |Keywords
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Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Chromatography, Gel; Chromatography, Ion Exchange; Dihydropteridine Reductase; Escherichia coli/enzymology; Escherichia coli Proteins; FMN Reductase; Flavin Mononucleotide/metabolism; Flavins/metabolism; Hemeproteins/isolation & purification; Hemeproteins/metabolism; Kinetics; NADH, NADPH Oxidoreductases/isolation & purification; NADH, NADPH Oxidoreductases/metabolism; Oxidation-Reduction
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8292013 PubMed]
 
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status
 
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Latest revision as of 04:53, 15 September 2013

Citation

Eschenbrenner, M, Coves, J and Fontecave, M (1994) Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein. Biochem. Biophys. Res. Commun. 198:127-31

Abstract

The haemoglobin-like protein (HMP) of E. coli previously isolated as a dihydropteridine reductase was shown to be also a ferric citrate reductase. We demonstrate that, in fact, HMP is a flavin reductase and that its ferric reductase activity is a result of its ability to reduce free flavins. However, when compared to the two main ferric/flavin reductases of E. coli, i.e., the NAD(P)H: flavin oxidoreductase and the sulfite reductase, one can conclude that the contribution of HMP to iron reduction is negligible.

Links

PubMed

Keywords

Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Chromatography, Gel; Chromatography, Ion Exchange; Dihydropteridine Reductase; Escherichia coli/enzymology; Escherichia coli Proteins; FMN Reductase; Flavin Mononucleotide/metabolism; Flavins/metabolism; Hemeproteins/isolation & purification; Hemeproteins/metabolism; Kinetics; NADH, NADPH Oxidoreductases/isolation & purification; NADH, NADPH Oxidoreductases/metabolism; Oxidation-Reduction

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