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Structural analysis of compound I in hemoproteins: Study on Proteus mirabilis catalase
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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1997 (English)In: BIOCHIMIE, ISSN 0300-9084, Vol. 79, no 11, 667-671 p.Article in journal (Refereed) Published
Abstract [en]

Ferryl catalysis has attracted considerable interest, because a diverse variety of enzymes use ferryl intermediates to perform difficult chemistry. The structure of the reactional intermediate compound I of Proteus mirabilis catalase (PMC) has been solve

Place, publisher, year, edition, pages
EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER , 1997. Vol. 79, no 11, 667-671 p.
Keyword [en]
catalase compound I; time-resolved crystallography; X-ray structure; BOVINE LIVER CATALASE; PR CATALASE; BOUND NADPH; CRYSTAL-STRUCTURE; PEROXIDASE; CRYSTALLOGRAPHY; MECHANISM; RADICALS; ENDOR; TIME
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-84804OAI: oai:DiVA.org:uu-84804DiVA: diva2:112712
Note
Addresses: Jouve HM, CEA, CNRS, Inst Biol Struct Jean Pierre Ebel, 41 Rue Martyrs, F-38027 Grenoble 01, France. CEA, CNRS, Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble 01, France. Univ Oxford, Mol Biophys Lab, Oxford OX1 3QU, England. Univ Oxford,Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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