Academic Journal
Vanadium haloperoxidases: from the discovery 30 years ago to X-Ray crystallographic and V K-edge absorption spectroscopic studies
| العنوان: | Vanadium haloperoxidases: from the discovery 30 years ago to X-Ray crystallographic and V K-edge absorption spectroscopic studies |
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| المؤلفون: | Leblanc, C, Vilter, H, Fournier, J.-B, Delage, L, Potin, P, Rebuffet, E, Michel, G, Solari, P.-L., Feiters, Mc, Czjzek, M |
| المساهمون: | Laboratoire de Biologie Intégrative des Modèles Marins (LBI2M), Station biologique de Roscoff Roscoff (SBR), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Zurmaiener Strasse, Centre de Recherche en Cancérologie de Marseille (CRCM), Aix Marseille Université (AMU)-Institut Paoli-Calmettes (IPC), Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Synchrotron SOLEIL (SSOLEIL), Centre National de la Recherche Scientifique (CNRS), Department Organic Chemistry, Radboud University Nijmegen |
| المصدر: | ISSN: 0010-8545. |
| بيانات النشر: | HAL CCSD Elsevier |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | X-ray absorption spectroscopy on biological vanadium, Oligomeric state, Structural evolution, Vanadium coordination, Crystallographic structure, Vanadium-dependent haloperoxidase, [CHIM]Chemical Sciences |
| الوصف: | International audience ; In the environment, vanadium-dependent haloperoxidases (VHPO) are likely to play a key role in the production of biogenic organo-halogens. These enzymes contain vanadate as a prosthetic group, and catalyze, in the presence of hydrogen peroxide, the oxidation of halide ions (Cl−, Br− or I−). They are classified according to the most electronegative halide that they can oxidize. Since the first discovery of a vanadium bromoperoxidase in the brown alga Ascophyllum nodosum thirty years ago, structural and mechanistic studies have been mainly conducted on two types of VHPO, chloro- and bromoperoxidases, and more recently on a vanadium-dependent iodoperoxidase. In this review, we highlight the main progress obtained on the structure-function relation of these proteins, based on biochemistry, crystallography and X-ray absorption spectroscopy (XAS). The comparison of 3D protein structures of the different VHPO helped identify the residues that govern the molecular mechanisms of catalysis and specificity of VHPO. Vanadium K-edge XAS gave further important insight to understand the fine changes around the vanadium cofactor during the catalytic cycle. The combination of different structural approaches, at different scales of resolution, shed new light on biological vanadium coordination in the active site, and its importance for the catalytic cycle and halide specificity of vanadium haloperoxidases. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | hal-01121900; https://hal.sorbonne-universite.fr/hal-01121900; https://hal.sorbonne-universite.fr/hal-01121900/document; https://hal.sorbonne-universite.fr/hal-01121900/file/Leblanc_Vanadium.pdf |
| DOI: | 10.1016/j.ccr.2015.02.013 |
| الاتاحة: | https://hal.sorbonne-universite.fr/hal-01121900 https://hal.sorbonne-universite.fr/hal-01121900/document https://hal.sorbonne-universite.fr/hal-01121900/file/Leblanc_Vanadium.pdf https://doi.org/10.1016/j.ccr.2015.02.013 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.FF7AE6F |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.ccr.2015.02.013 |
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