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Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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1996 (English)In: NATURE STRUCTURAL BIOLOGY, ISSN 1072-8368, Vol. 3, no 11, 951-956 p.Article in journal (Refereed) Published
Abstract [en]

Various enzymes use semi-stable ferryl intermediates and free radicals during their catalytic cycle, amongst them haem catalases. Structures for two transient intermediates (compounds I and II) of the NADPH-dependent catalase from Proteus mirabilis (PMC)

Place, publisher, year, edition, pages
NATURE PUBLISHING CO , 1996. Vol. 3, no 11, 951-956 p.
Keyword [en]
PEROXIDASE COMPOUND-I; MIRABILIS PR CATALASE; 3-DIMENSIONAL STRUCTURE; CRYSTAL-STRUCTURE; LIVER CATALASE; BOUND NADPH; RESOLUTION; PROTEIN; MECHANISM; CATALYSIS
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-28310OAI: oai:DiVA.org:uu-28310DiVA: diva2:56206
Note
Addresses: Gouet P, UNIV OXFORD, MOL BIOPHYS LAB, S PARKS RD, OXFORD OX1 3QU, ENGLAND. UNIV OXFORD, OXFORD CTR MOL SCI, OXFORD OX1 3QU, ENGLAND. CEA, CNRS, INST BIOL STRUCT JEAN PIERRE EBEL, ENZYMOL LAB, F-38027 GRENOBLE 1, FRANCE. SWEDISH UNIV AGR SCI, UAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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