Literature DB >> 11761334

Reduced flavin: donor and acceptor enzymes and mechanisms of channeling.

S C Tu1.   

Abstract

Although mechanisms of metabolite channeling have been extensively studied, the nature of reduced flavin transfer from donor to acceptor enzymes remains essentially unexplored. In this review, identities and properties of reduced flavin-producing enzymes (namely flavin reductases) and reduced flavin-requiring processes and enzymes are summarized. By using flavin reductase-luciferase enzyme couples from luminous bacteria, two types of reduced flavin channeling were observed involving the differential transfers of the reduced flavin cofactor and the reduced flavin product of reductase to luciferase. The exact mode of transfer is controlled by the specific makeup of the constituent enzymes within the reductase-luciferase couple. The plausible physiological significance of the monomer-dimer equilibrium of the NADPH-specific flavin reductase from Vibrio harveyi is also discussed.

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Year:  2001        PMID: 11761334     DOI: 10.1089/15230860152665046

Source DB:  PubMed          Journal:  Antioxid Redox Signal        ISSN: 1523-0864            Impact factor:   8.401


  18 in total

1.  Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli.

Authors:  Kholis Abdurachim; Holly R Ellis
Journal:  J Bacteriol       Date:  2006-09-22       Impact factor: 3.490

2.  Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli.

Authors:  Benlian Gao; Adam Bertrand; William H Boles; Holly R Ellis; T Conn Mallett
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2005-08-31

3.  Evaluation of the Conformational Stability of Recombinant Desulfurizing Enzymes from a Newly Isolated Rhodococcus sp.

Authors:  Federica Parravicini; Stefania Brocca; Marina Lotti
Journal:  Mol Biotechnol       Date:  2016-01       Impact factor: 2.695

4.  Structural basis of free reduced flavin generation by flavin reductase from Thermus thermophilus HB8.

Authors:  Takahito Imagawa; Toshiharu Tsurumura; Yasushi Sugimoto; Kenji Aki; Kazumi Ishidoh; Seiki Kuramitsu; Hideaki Tsuge
Journal:  J Biol Chem       Date:  2011-11-03       Impact factor: 5.157

5.  BluB cannibalizes flavin to form the lower ligand of vitamin B12.

Authors:  Michiko E Taga; Nicholas A Larsen; Annaleise R Howard-Jones; Christopher T Walsh; Graham C Walker
Journal:  Nature       Date:  2007-03-22       Impact factor: 49.962

6.  Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity.

Authors:  Sarayut Nijvipakul; David P Ballou; Pimchai Chaiyen
Journal:  Biochemistry       Date:  2010-11-02       Impact factor: 3.162

7.  LuxG is a functioning flavin reductase for bacterial luminescence.

Authors:  Sarayut Nijvipakul; Janewit Wongratana; Chutintorn Suadee; Barrie Entsch; David P Ballou; Pimchai Chaiyen
Journal:  J Bacteriol       Date:  2007-12-21       Impact factor: 3.490

8.  Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions.

Authors:  Hiroaki Iwaki; Stephan Grosse; Hélène Bergeron; Hannes Leisch; Krista Morley; Yoshie Hasegawa; Peter C K Lau
Journal:  Appl Environ Microbiol       Date:  2013-03-22       Impact factor: 4.792

9.  Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates.

Authors:  Zachary T Campbell; Thomas O Baldwin
Journal:  J Biol Chem       Date:  2009-08-26       Impact factor: 5.157

10.  Fre Is the Major Flavin Reductase Supporting Bioluminescence from Vibrio harveyi Luciferase in Escherichia coli.

Authors:  Zachary T Campbell; Thomas O Baldwin
Journal:  J Biol Chem       Date:  2009-01-12       Impact factor: 5.157

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