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Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd(1) nitrite reductase
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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2001 (English)In: JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, Vol. 276, no 8, 5846-5855 p.Article in journal (Refereed) Published
Abstract [en]

The heme ligation in the isolated c domain of Paracoccus pantotrophus cytochrome ed, nitrite reductase has been characterized in both oxidation states in solution by NMR spectroscopy. In the reduced form, the heme ligands are His(69)-Met(106), and the ter

Place, publisher, year, edition, pages
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC , 2001. Vol. 276, no 8, 5846-5855 p.
Keyword [en]
PARACOCCUS-PANTOTROPHUS; LIGAND-EXCHANGE; YEAST ISO-1-CYTOCHROME-C; MAGNETIC-RESONANCE; CHEMICAL-SHIFTS; ACTIVE-SITES; SPECTROSCOPY; IDENTIFICATION; PROTEINS; COOA
Identifiers
URN: urn:nbn:se:uu:diva-38038OAI: oai:DiVA.org:uu-38038DiVA: diva2:65937
Note
Addresses: Steensma E, Univ Uppsala, Dept Biochem, Box 576, S-75123 Uppsala, Sweden. Univ Uppsala, Dept Biochem, S-75123 Uppsala, Sweden. Univ Oxford, Dept Biochem, Oxford OX1 3QU, England.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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