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N-terminal arm exchange is observed in the 2.15 angstrom crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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1997 (English)In: STRUCTURE, ISSN 0969-2126, Vol. 5, no 9, 1157-1171 p.Article in journal (Refereed) Published
Abstract [en]

Background: Nitrite reductase from Pseudomonas aeruginosa (NiR-Pa) is a dimer consisting of two identical 60 kDa subunits, each of which contains one c and one d(1) heme group. This enzyme, a soluble component of the electron-transfer chain that uses nit

Place, publisher, year, edition, pages
CURRENT BIOLOGY LTD , 1997. Vol. 5, no 9, 1157-1171 p.
Keyword [en]
crystal structure; denitrification; domain swapping; electron transfer; nitrite reductase; Pseudomonas aeruginosa; CYTOCHROME-OXIDASE; ELECTRON-TRANSFER; PURIFICATION PROCEDURE; LIGAND-BINDING; PROTEIN MODELS; RESOLUTION; REFINEMENT; CRYSTALLIZATION; DE
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-77696OAI: oai:DiVA.org:uu-77696DiVA: diva2:105608
Note
Addresses: IBSM, UPR 9039 CNRS, MARSEILLE 20, FRANCE. UNIV ROMA LA SAPIENZA, DIPARTIMENTO SCI BIOCHIM, I-00185 ROME, ITALY. EUROPEAN SYNCHROTRON RADIAT FACIL, F-38043 GRENOBLE, FRANCE. UNIV OXFORD, MOL BIOPHYS LAB, OXFORD OX1 3QU, ENGLAND. UNIV OXFORD, OAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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