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FMN reductase
Known as:
Oxidoreductase, FMN
, NAD(P)H-FMN Oxidoreductase
, Reductase, Flavin Mononucleotide
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An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their…
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National Institutes of Health
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Related topics
Related topics
23 relations
Chronic granulomatous disease
Electron Transport
Electron Transport Complex I
In Blood
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Narrower (4)
Cytochrome c Reductase
Fre protein, E coli
NADPH Dehydrogenase
ferric citrate iron reductase
Broader (3)
Iron-Sulfur Proteins
NADH, NADPH Oxidoreductases
respiratory enzyme
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2006
2006
Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.
R. Agarwal
,
J. Bonanno
,
S. Burley
,
S. Swaminathan
Acta Crystallographica Section D: Biological…
2006
Corpus ID: 24638854
The availability of high-intensity synchrotron facilities, technological advances in data-collection techniques and improved data…
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1983
1983
Automated bioluminescent assays for NADH, glucose 6-phosphate, primary bile acids, and ATP.
L. Kricka
,
G. Wienhausen
,
J. Hinkley
,
M. De Luca
Analytical Biochemistry
1983
Corpus ID: 36396689
Highly Cited
1983
Highly Cited
1983
Transient kinetics of redox reactions of flavodoxin: effects of chemical modification of the flavin mononucleotide prosthetic group on the dynamics of intermediate complex formation and electron…
R. Simondsen
,
G. Tollin
Biochemistry
1983
Corpus ID: 46678204
The effects of structural modifications of the flavin mononucleotide (FMN) prosthetic group of Clostridium pasteurianum…
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Highly Cited
1982
Highly Cited
1982
Bioluminescence measurement of primary bile acids using immobilized 7 alpha-hydroxysteroid dehydrogenase: application to serum bile acids.
A. Roda
,
L. Kricka
,
M. Deluca
,
A. Hofmann
Journal of Lipid Research
1982
Corpus ID: 12730467
A simple, rapid, and sensitive bioluminescence method for measuring primary bile acids has been developed and validated. The…
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1982
1982
A sensitive bioluminescent immunoassay for dinitrophenol and trinitrotoluene.
J. Wannlund
,
M. Deluca
Analytical Biochemistry
1982
Corpus ID: 46285410
1978
1978
Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis.
D. J. Steenkamp
,
T. Singer
Biochemical Journal
1978
Corpus ID: 26972787
Bacterial trimethylamine dehydrogenase contains a novel type of covalently bound flavin mononucleotide and a tetrameric iron…
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1976
1976
Immobilization of bacterial luciferase and FMN reductase on glass rods.
E. Jablonski
,
M. Deluca
Proceedings of the National Academy of Sciences…
1976
Corpus ID: 24087432
Bacterial luciferase and NAD(P)H: FMN oxidoreductase isolated from Beneckea harveyi were covalently linked via diazotization to…
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Review
1970
Review
1970
Regulation of flavoprotein enzymes in hypothyroidism and in riboflavin deficiency.
R. Rivlin
Advances in Enzyme Regulation
1970
Corpus ID: 28926230
Highly Cited
1969
Highly Cited
1969
The effect of flavin isomers and analogues upon the color of bacterial bioluminescence.
G. Mitchell
,
J. W. Hastings
Journal of Biological Chemistry
1969
Corpus ID: 1079491
Highly Cited
1963
Highly Cited
1963
Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide.
Hastings Jw
,
Gibson Qh
1963
Corpus ID: 80963041
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