ArticleProtein science : a publication of the Protein Society2016
Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis.
Article in Protein science : a publication of the Protein Society, 2016. 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, 41 citations in OpenAlex.
- Construction and immunogenicity evaluation of a tuberculosis subunit vaccine based on fusion protein AP2 and novel adjuvant ASM.Archives of microbiology · 2026Article
- The terminal heme synthetic enzyme, coproheme decarboxylase, negatively regulates heme uptake in Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Article
- Heme disposal inside heart transplants: a trigger for rejection?The Journal of clinical investigation · 2026Article
- Systemic engineering and global regulation enabling high-level bilirubin biosynthesis.Nature communications · 2025Article
- Exploring Large Protein Sequence Space through Homology- and Representation-based Hierarchical Clustering.Molecular biology and evolution · 2025Article
- Functions of nitroreductases in mycobacterial physiology and drug susceptibility.Journal of bacteriology · 2025Review
- The radical scavenging activity of 1-methyl-1,4-dihydronicotinamide: theoretical insights into the mechanism, kinetics and solvent effects.RSC advances · 2024Article
- Loss of Biliverdin Reductase Increases Oxidative Stress in the CyanobacteriumMicroorganisms · 2023Article
- Production of copropophyrin III, biliverdin and bilirubin by the rufomycin producer,Frontiers in microbiology · 2023Article
- Cofactor F420: an expanded view of its distribution, biosynthesis and roles in bacteria and archaea.FEMS microbiology reviews · 2021Article
- Article
- Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures.Current medicinal chemistry · 2020Review
- Structure of aBiochemistry · 2019Article
- FAD-sequestering proteins protect mycobacteria against hypoxic and oxidative stress.The Journal of biological chemistry · 2019Article
- Heme Uptake and Utilization by Gram-Negative Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2019Review
- Biosynthesis of the Thiopeptins and Identification of an FJournal of the American Chemical Society · 2018Article
- Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence-Function Space and Genome Context to Discover Novel Functions.Biochemistry · 2017Review
- Enzymatic Activity and Thermodynamic Stability of Biliverdin IXβ Reductase Are Maintained by an Active Site Serine.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Cofactor Tail Length Modulates Catalysis of Bacterial FFrontiers in microbiology · 2017Article
- Mycobacterial FFrontiers in microbiology · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bilirubin is a potent antioxidant that is produced from the reduction of the heme degradation product biliverdin. In mammalian cells and Cyanobacteria, NADH/NADPH-dependent biliverdin reductases (BVRs) of the Rossmann-fold have been shown to catalyze this reaction. Here, we describe the characterization of Rv2074 from Mycobacterium tuberculosis, which belongs to a structurally and mechanistically distinct family of F420 H2 -dependent BVRs (F-BVRs) that are exclusively found in Actinobacteria. We have solved the crystal structure of Rv2074 bound to its cofactor, F420 , and used this alongside molecular dynamics simulations, site-directed mutagenesis and NMR spectroscopy to elucidate its catalytic mechanism. The production of bilirubin by Rv2074 could exploit the anti-oxidative properties of bilirubin and contribute to the range of immuno-evasive mechanisms that have evolved in M. tuberculosis to allow persistent infection.
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