Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action-Reference-Cited by-同舟云学术

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Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action

Published:2004-03 Issue:13 Volume:279 Page:12860-12867
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

van den Heuvel Robert H.H.,Westphal Adrie H.,Heck Albert J.R.,Walsh Martin A.,Rovida Stefano,van Berkel Willem J.H.,Mattevi Andrea

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

1. NAD(P)H:flavin oxidoreductase of Escherichia coli. A ferric iron reductase participating in the generation of the free radical of ribonucleotide reductase.

2. Reduction and mobilization of iron by a NAD(P)H: flavin oxidoreductase from Escherichia coli

3. Differential Transfers of Reduced Flavin Cofactor and Product by Bacterial Flavin Reductase to Luciferase

4. Identification of the gene encoding the major NAD(P)H-flavin oxidoreductase of the bioluminescent bacterium Vibrio fischeri ATCC 7744

5. Crystal Structure of NAD(P)H:Flavin Oxidoreductase from Escherichia coli,

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2. Flavin-Dependent Monooxygenases Involved in Bacterial Degradation of Chlorophenols;Applied Biochemistry and Microbiology;2022-12

3. On the diversity of F 420 ‐dependent oxidoreductases: A sequence‐ and structure‐based classification;Proteins: Structure, Function, and Bioinformatics;2021-07-16

4. Steady-state kinetic analysis of halogenase-supporting flavin reductases BorF and AbeF reveals different kinetic mechanisms;Archives of Biochemistry and Biophysics;2021-06

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