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dc.contributor.authorGräwert, Tobias
dc.contributor.authorRohdich, Felix
dc.contributor.authorSpan, Lngrid
dc.contributor.authorBacker, Adelbert
dc.contributor.authorEisenreich, Wolfgang
dc.contributor.authorEppinger, Jörg
dc.contributor.authorGroll, Michael
dc.date.accessioned2015-08-02T09:10:59Z
dc.date.available2015-08-02T09:10:59Z
dc.date.issued2009-07-20
dc.identifier.issn14337851
dc.identifier.pmid19569147
dc.identifier.doi10.1002/anie.200900548
dc.identifier.urihttp://hdl.handle.net/10754/561426
dc.description.abstractThe terminal step of the non-mevalonate pathway of terpene biosynthesis is catalyzed by IspH (see scheme). In the crystal structure of IspH from E. coli, a bound inorganic diphosphate ligand occupies the position of the diphosphate residue of the substrate. Together with mutation studies and theoretical calculations, these data support a mechanism which is analogous to the Birch reduction of allylic alcohols. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.
dc.publisherWiley-Blackwell
dc.subjectEnzymes
dc.subjectIron-sulfur clusters
dc.subjectIsoprenes
dc.subjectNon-mevalonate pathway
dc.subjectReaction mechanisms
dc.titleStructure of active IspH enzyme from escherichia coli provides mechanistic insights into substrate reduction
dc.typeArticle
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentPhysical Sciences and Engineering (PSE) Division
dc.contributor.departmentChemical Science Program
dc.contributor.departmentBiological & Organometallic Catalysis Laboratories
dc.identifier.journalAngewandte Chemie International Edition
dc.contributor.institutionCenter for Integrated Protein Science, Lehrstuhl für Biochemie Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany
dc.contributor.institutionDepartment Chemie Technische, Universität München, Germany
kaust.personEppinger, Jörg


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