ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2005
Vanadium-dependent iodoperoxidases in Laminaria digitata, a novel biochemical function diverging from brown algal bromoperoxidases.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 84 citations in OpenAlex.
- Novel vanadium-dependent haloperoxidases from macroalgae and their expression in response to biotic and abiotic stressors inMarine life science & technology · 2026Article
- Vanadium-Dependent Haloperoxidase Gene Evolution in Brown Algae: Evidence for Horizontal Gene Transfer.International journal of molecular sciences · 2025Article
- 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
- Review
- New Aspects of Uptake and Metabolism of Non-organic and Organic Iodine Compounds-The Role of Vanadium and Plant-Derived Thyroid Hormone Analogs in Lettuce.Frontiers in plant science · 2021Article
- Single-base methylome profiling of the giant kelp Saccharina japonica reveals significant differences in DNA methylation to microalgae and plants.The New phytologist · 2020Article
- Emission of volatile halogenated compounds, speciation and localization of bromine and iodine in the brown algal genome model Ectocarpus siliculosus.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Environmental Control of Vanadium Haloperoxidases and Halocarbon Emissions in Macroalgae.Marine biotechnology (New York, N.Y.) · 2018Review
- Saccharina genomes provide novel insight into kelp biology.Nature communications · 2015Article
- Preferential expression of a bromoperoxidase in sporophytes of a red alga, Pyropia yezoensis.Marine biotechnology (New York, N.Y.) · 2015Article
- 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.Applied and environmental microbiology · 2014Article
- Chemical and enzymatic fractionation of cell walls from Fucales: insights into the structure of the extracellular matrix of brown algae.Annals of botany · 2014Article
- Iodine contributes to osmotic acclimatisation in the kelp Laminaria digitata (Phaeophyceae).Planta · 2014Article
- In vivo speciation studies and antioxidant properties of bromine in Laminaria digitata reinforce the significance of iodine accumulation for kelps.Journal of experimental botany · 2013Article
- The halogenated metabolism of brown algae (Phaeophyta), its biological importance and its environmental significance.Marine drugs · 2010Review
- Microchemical imaging of iodine distribution in the brown alga Laminaria digitata suggests a new mechanism for its accumulation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2008Article
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7 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The brown alga Laminaria digitata features a distinct vanadium-dependent iodoperoxidase (vIPO) activity, which has been purified to electrophoretic homogeneity. Steady-state analyses at pH 6.2 are reported for vIPO (K (m) (I-) = 2.5 mM; k (cat) (I-) = 462 s(-1)) and for the previously characterised vanadium-dependent bromoperoxidase in L. digitata (K (m) (I-) =18.1 mM; k (cat) (I-) = 38 s(-1)). Although the vIPO enzyme specifically oxidises iodide, competition experiments with halides indicate that bromide is a competitive inhibitor with respect to the fixation of iodide. A full-length complementary ANA (cDNA) was cloned and shown to be actively transcribed in L. digitata and to encode the vIPO enzyme. Mass spectrometry analyses of tryptic digests of vIPO indicated the presence of at least two very similar proteins, in agreement with Southern analyses showing that vIPOs are encoded by a multigenic family in L. digitata. Phylogenetic analyses indicated that vIPO shares a close common ancestor with brown algal vanadium-dependent bromoperoxidases. Based on a three-dimensional structure model of the vIPO active site and on comparisons with those of other vanadium-dependent haloperoxidases, we propose a hypothesis to explain the evolution of strict specificity for iodide in L. digitata vIPO.
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