Lookup NU author(s): Dr Clive Butler
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The purification of small quantities of a major small c-type cytochrome from the anammox bacterium Kuenenia stuttgartiensis has recently been reported. In order to characterise this protein further we have expressed the gene encoding this cytochrome in Escherichia coli and have purified the protein to homogeneity. The protein is directed to the E. coli periplasm using its native signal sequence suggesting that it may be translocated via a Sec-type system in K. stuttgartiensis. The cytochrome has the visible spectroscopic properties typical of a low-spin c-type cytochrome, but these spectroscopic features broaden in high salt solutions. The oxidised cytochrome was able to bind the ligands NO and cyanide. A redox potential of +230 mV suggests that the protein is suitable to act as an electron carrier protein that may be involved in the respiratory chain between hydrazine oxidation and the reduction of nitrite. The predicted protein sequence for the cytochrome suggests it to be a predominantly α-helical protein, and this is supported by circular dichroism. © 2006 Elsevier Inc. All rights reserved.
Author(s): Huston WM, Harhangi HR, Leech AP, Butler CS, Jetten MSM, Op den Camp HJM, Moir JWB
Publication type: Article
Publication status: Published
Journal: Protein Expression and Purification
Print publication date: 01/01/2007
ISSN (print): 1046-5928
ISSN (electronic): 1096-0279
Publisher: Academic Press
PubMed id: 17049265
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