Iodine Bioinorganic Chemistry : Physiology, Structures, and Mechanisms

Zitieren

Dateien zu dieser Ressource

Dateien Größe Format Anzeige

Zu diesem Dokument gibt es keine Dateien.

KÜPPER, Frithjof C., Peter M. H. KRONECK, 2015. Iodine Bioinorganic Chemistry : Physiology, Structures, and Mechanisms. In: KAIHO, Tatsuo, ed.. Iodine chemistry and applications. Hoboken, NJ:Wiley, pp. 557-589. ISBN 978-1-118-46629-2

@incollection{Kupper2015Iodin-38949, title={Iodine Bioinorganic Chemistry : Physiology, Structures, and Mechanisms}, year={2015}, doi={10.1002/9781118909911.ch32}, isbn={978-1-118-46629-2}, address={Hoboken, NJ}, publisher={Wiley}, booktitle={Iodine chemistry and applications}, pages={557--589}, editor={Kaiho, Tatsuo}, author={Küpper, Frithjof C. and Kroneck, Peter M. H.} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/38949"> <dcterms:title>Iodine Bioinorganic Chemistry : Physiology, Structures, and Mechanisms</dcterms:title> <dc:creator>Kroneck, Peter M. H.</dc:creator> <dc:contributor>Küpper, Frithjof C.</dc:contributor> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-17T13:43:12Z</dcterms:available> <dc:contributor>Kroneck, Peter M. H.</dc:contributor> <dcterms:abstract xml:lang="eng">Iodine occurs as iodide in seawater and is taken up by seaweed, from which it has traditionally been extracted. This chapter discusses the manifold roles of iodine and a prominent member of the halogen element family. Emphasis is laid on bioinorganic aspects of iodine compounds including the transformation of hypoiodite by vanadium-dependent enzymes. The chapter highlights the structure and function of these enzymes. Vanadium is the second most abundant transition metal in seawater and universally distributed in the soil, and constitutes an inherent part of important enzymatic active sites; the most prominent examples are vanadium haloperoxidases (V-HPO) and vanadium nitrogenase. Structural and biochemical researches have focused on residues to the vicinity of the active site in V-dependent chloroperoxidases (V-CPO), vanadium bromoperoxidase (V-BPO), and vanadium iodoperoxidases (V-IPO), which could explain the origin of halide selectivity.</dcterms:abstract> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38949"/> <dc:creator>Küpper, Frithjof C.</dc:creator> <dcterms:issued>2015</dcterms:issued> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-17T13:43:12Z</dc:date> </rdf:Description> </rdf:RDF>

Das Dokument erscheint in:

KOPS Suche


Stöbern

Mein Benutzerkonto