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The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2001 (English)In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ISSN 0006-291X, Vol. 281, no 3, 788-794 p.Article in journal (Refereed) Published
Abstract [en]

Cytochrome cd(1) nitrite reductase from Paracoccus pantotrophus is a dimer; within each monomer there is a largely alpha-helical domain that contains the c-type cytochrome centre. The structure of this domain changes significantly upon reduction of the he

Place, publisher, year, edition, pages
ACADEMIC PRESS INC , 2001. Vol. 281, no 3, 788-794 p.
Keyword [en]
cytochrome cd(1); Paracoccus pantotrophus; nitrite reductase; cytochrome biogenesis; NITRITE REDUCTASE; PSEUDOMONAS-AERUGINOSA; HETEROLOGOUS EXPRESSION; C(552); BIOGENESIS; K-12; PURIFICATION; PERIPLASM; BACTERIA; OXIDASE
URN: urn:nbn:se:uu:diva-38014OAI: oai:DiVA.org:uu-38014DiVA: diva2:65913
Addresses: Ferguson SJ, Univ Oxford, Dept Biochem, S Parks Rd, Oxford OX1 3QU, England. Univ Oxford, Dept Biochem, Oxford OX1 3QU, England. Univ Uppsala, Dept Biochem, S-75123 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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