Conformational transitions induced by NADH binding promote reduction half-reaction in 2-hydroxybiphenyl-3-monooxygenase catalytic cycle
Author:
Funder
Lomonosov Moscow State University
Russian Science Foundation
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference29 articles.
1. Form follows function: structural and catalytic variation in the class A flavoprotein monooxygenases;Crozier-Reabe;Int. J. Mol. Sci.,2012
2. Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1;Suske;J. Biol. Chem.,1999
3. Preparative application of 2-hydroxybiphenyl 3-monooxygenase with enzymatic cofactor regeneration in organic-aqueous reaction media;Lutz;J. Mol. Catal. B Enzym.,2002
4. Changing the substrate reactivity of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica HBP1 by directed evolution;Meyer;J. Biol. Chem.,2002
5. Preparative scale production of 3-substituted catechols using a novel monooxygenase from Pseudomonas azelaica HBP 1;Held;J. Mol. Catal. B Enzym.,1998
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