ArticleThe Journal of biological chemistry2009
Fre Is the Major Flavin Reductase Supporting Bioluminescence from Vibrio harveyi Luciferase in Escherichia coli.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Autonomous Bioluminescence Systems: From Molecular Mechanisms to Emerging Applications.JACS Au · 2025Review
- The Role of Dioxygen in Microbial Bio-Oxygenation: Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme.Microorganisms · 2024Review
- Complete Biochemical Characterization of Pantaphos Biosynthesis Highlights an Unusual Role for a SAM-Dependent Methyltransferase.Angewandte Chemie (International ed. in English) · 2024Article
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (International ed. in English) · 2023Article
- Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Inter-Species Redox Coupling by Flavin Reductases and FMN-Dependent Two-Component Monooxygenases Undertaking Nucleophilic Baeyer-Villiger Biooxygenations.Microorganisms · 2022Article
- Generation of bright autobioluminescent bacteria by chromosomal integration of the improved lux operon ilux2.Scientific reports · 2022Article
- Article
- Molecular Mechanisms of Bacterial Bioluminescence.Computational and structural biotechnology journal · 2018Review
- Reply to the Comment by Littlechild and Isupov.Microorganisms · 2017Article
- Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.Chemical reviews · 2017Review
- Re-wiring of energy metabolism promotes viability during hyperreplication stress in E. coli.PLoS genetics · 2017Article
- Flavin-Dependent Redox Transfers by the Two-Component Diketocamphane Monooxygenases of Camphor-Grown Pseudomonas putida NCIMB 10007.Microorganisms · 2016Article
- Promising Biological Indicator of Heavy Metal Pollution: Bioluminescent Bacterial Strains Isolated and Characterized from Marine Niches of Goa, India.Indian journal of microbiology · 2015Article
- A protein-RNA specificity code enables targeted activation of an endogenous human transcript.Nature structural & molecular biology · 2014Article
- The bacterial redox signaller pyocyanin as an antiplasmodial agent: comparisons with its thioanalog methylene blue.Redox report : communications in free radical research · 2011Article
- Reduction kinetics of a flavin oxidoreductase LuxG from Photobacterium leiognathi (TH1): half-sites reactivity.Biochemistry · 2010Article
- Article
- Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD oxidoreductase (TftC) of Burkholderia cepacia AC1100.The Journal of biological chemistry · 2010Article
- Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike the vast majority of flavoenzymes, bacterial luciferase requires an exogenous source of reduced flavin mononucleotide for bioluminescence activity. Within bioluminescent bacterial cells, species-specific oxidoreductases are believed to provide reduced flavin for luciferase activity. The source of reduced flavin in Escherichia coli-expressing bioluminescence is not known. There are two candidate proteins potentially involved in this process in E. coli, a homolog of the Vibrio harveyi Frp oxidoreductase, NfsA, and a luxG type oxidoreductase, Fre. Using single gene knock-out strains, we show that deletion of fre decreased light output by greater than two orders of magnitude, yet had no effect on luciferase expression in E. coli. Purified Fre is capable of supporting bioluminescence in vitro with activity comparable to that with the endogenous V. harveyi reductase (Frp), using either FMN or riboflavin as substrate. In a pull-down experiment, we found that neither Fre nor Frp co-purify with luciferase. In contrast to prior work, we find no evidence for stable complex formation between luciferase and oxidoreductase. We conclude that in E. coli, an enzyme primarily responsible for riboflavin reduction (Fre) can also be utilized to support high levels of bioluminescence.
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