Mapping the Interactions between Flavodoxin and Its Physiological Partners Flavodoxin Reductase and Cobalamin-Dependent Methionine Synthase

Flavodoxins are electron-transfer proteins that contain the prosthetic group flavin mononucleotide. In Escherichia coli, flavodoxin is reduced by the FAD-containing protein NADPH:ferredoxin (flavodoxin) oxidoreductase; flavodoxins serve as electron donors in the reductive activation of anaerobic rib...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2001-08, Vol.98 (17), p.9521-9526
Main Authors: Hall, Diane A., Craig W. Vander Kooi, Stasik, Chad N., Stevens, Shawn Y., Erik R. P. Zuiderweg, Matthews, Rowena G.
Format: Article
Language:English
Subjects:
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - chemistry
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase - metabolism
Amides
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding Sites
Biochemistry
Biological Sciences
Chemical equilibrium
Cobalamin-dependent methionine synthase
Cytochromes
Electron transfer
Electronic structure
Electrons
Enzymes
Escherichia coli
Escherichia coli - chemistry
Face
ferredoxin
flavodoxin
Flavodoxin - chemistry
Flavodoxin - metabolism
flavodoxin reductase
Magnetic Resonance Spectroscopy
methionine synthase
Models, Molecular
NADH, NADPH Oxidoreductases - chemistry
NADH, NADPH Oxidoreductases - metabolism
NADPH
Oxidation-Reduction
Plasmids
Protein Binding
Protein Conformation
Proteins
S-Adenosylmethionine - metabolism
Titration
Vitamin B 12 - metabolism
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Summary:Flavodoxins are electron-transfer proteins that contain the prosthetic group flavin mononucleotide. In Escherichia coli, flavodoxin is reduced by the FAD-containing protein NADPH:ferredoxin (flavodoxin) oxidoreductase; flavodoxins serve as electron donors in the reductive activation of anaerobic ribonucleotide reductase, biotin synthase, pyruvate formate lyase, and cobalamin-dependent methionine synthase. In addition, domains homologous to flavodoxin are components of the multidomain flavoproteins cytochrome P450 reductase, nitric oxide synthase, and methionine synthase reductase. Although three-dimensional structures are known for many of these proteins and domains, very little is known about the structural aspects of their interactions. We address this issue by using NMR chemical shift mapping to identify the surfaces on flavodoxin that bind flavodoxin reductase and methionine synthase. We find that these physiological partners bind to unique overlapping sites on flavodoxin, precluding the formation of ternary complexes. We infer that the flavodoxin-like domains of the cytochrome P450 reductase family form mutually exclusive complexes with their electron-donating and -accepting partners, complexes that require conformational changes for interconversion.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.171168898