ArticleApplied and environmental microbiology2014
The Vanadium Iodoperoxidase from the marine flavobacteriaceae species Zobellia galactanivorans reveals novel molecular and evolutionary features of halide specificity in the vanadium haloperoxidase enzyme family.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 62 citations in OpenAlex.
- Novel vanadium-dependent haloperoxidases from macroalgae and their expression in response to biotic and abiotic stressors inMarine life science & technology · 2026Article
- Mechanistic Insights and Catalytic Efficiency of a 2,2'-Bipyridine-Coordinated Peroxidovanadium Complex as a Haloperoxidase Biomimetic.ChemPlusChem · 2025Article
- Separation of halide oxidation and substrate halogenation chemistries rationalizes site-selective vanadium dependent haloperoxidase catalysis.bioRxiv : the preprint server for biology · 2025Article
- The induced-fit and catalytic mechanisms of human G6PC1.Cell discovery · 2025Article
- Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases.Nature communications · 2025Article
- Vanadium haloperoxidases as noncanonical terpene synthases.Methods in enzymology · 2024Article
- Heterologous Expression and Biochemical Characterization of a New Chloroperoxidase Isolated from the Deep-Sea Hydrothermal Vent Black Yeast Hortaea werneckii UBOCC-A-208029.Marine biotechnology (New York, N.Y.) · 2023Article
- Structural Basis of Stereospecific Vanadium-Dependent Haloperoxidase Family Enzymes in Napyradiomycin Biosynthesis.Biochemistry · 2022Article
- Consuming fresh macroalgae induces specific catabolic pathways, stress reactions and Type IX secretion in marine flavobacterial pioneer degraders.The ISME journal · 2022Article
- Halogenation in Fungi: What Do We Know and What Remains to Be Discovered?Molecules (Basel, Switzerland) · 2022Review
- Halogenases: a palette of emerging opportunities for synthetic biology-synthetic chemistry and C-H functionalisation.Chemical Society reviews · 2021Review
- Functional Characterization of a L-2-Haloacid Dehalogenase FromFrontiers in microbiology · 2021Article
- Proteomic enzyme analysis of the marine fungus Paradendryphiella salina reveals alginate lyase as a minimal adaptation strategy for brown algae degradation.Scientific reports · 2019Article
- Crystal structure and biochemical characterization of the transmembrane PAP2 type phosphatidylglycerol phosphate phosphatase from Bacillus subtilis.Cellular and molecular life sciences : CMLS · 2017Article
- Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.Chemical reviews · 2017Review
- Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-Accumulating Bacterium Isolated from Surface Marine Sediment.Genome announcements · 2016Article
- Article
- Use of Iodine to Biofortify and Promote Growth and Stress Tolerance in Crops.Frontiers in plant science · 2016Review
- Saccharina genomes provide novel insight into kelp biology.Nature communications · 2015Article
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vanadium haloperoxidases (VHPO) are key enzymes that oxidize halides and are involved in the biosynthesis of organo-halogens. Until now, only chloroperoxidases (VCPO) and bromoperoxidases (VBPO) have been characterized structurally, mainly from eukaryotic species. Three putative VHPO genes were predicted in the genome of the flavobacterium Zobellia galactanivorans, a marine bacterium associated with macroalgae. In a phylogenetic analysis, these putative bacterial VHPO were closely related to other VHPO from diverse bacterial phyla but clustered independently from eukaryotic algal VBPO and fungal VCPO. Two of these bacterial VHPO, heterogeneously produced in Escherichia coli, were found to be strictly specific for iodide oxidation. The crystal structure of one of these vanadium-dependent iodoperoxidases, Zg-VIPO1, was solved by multiwavelength anomalous diffraction at 1.8 Å, revealing a monomeric structure mainly folded into α-helices. This three-dimensional structure is relatively similar to those of VCPO of the fungus Curvularia inaequalis and of Streptomyces sp. and is superimposable onto the dimeric structure of algal VBPO. Surprisingly, the vanadate binding site of Zg-VIPO1 is strictly conserved with the fungal VCPO active site. Using site-directed mutagenesis, we showed that specific amino acids and the associated hydrogen bonding network around the vanadate center are essential for the catalytic properties and also the iodide specificity of Zg-VIPO1. Altogether, phylogeny and structure-function data support the finding that iodoperoxidase activities evolved independently in bacterial and algal lineages, and this sheds light on the evolution of the VHPO enzyme family.
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