Cytochromes P460 and c′-beta; A new family of high-spin cytochromes c

Edited by Stuart Ferguson

Received 11 January 2007; received in revised form 24 January 2007; accepted 25 January 2007. published online 05 February 2007.

Abstract

Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of N-oxides, are shown to represent an evolutionarily related new family of monoheme, ∼17kDa, cytochromes c found in the genomes of diverse Proteobacteria. All members of this family have a predicted secondary structure predominantly of beta-sheets in contrast to the predominantly alpha-helical cytochromes c′ found in photoheterotrophic and denitrifying Proteobacteria.

Keywords: Cytochrome c′, Cytochrome P460, Denitrification, N-oxide detoxification, Bacterial enzyme evolution

a Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, St. Paul, MN, United States

b Department of Biology, Black Hills State University, Spearfish, SD, United States

c Departments of Biology and Microbiology and Immunology, University of Louisville, Louisville, KY, United States

Corresponding author. Address: 140 Gortner Laboratory, 1479 Gortner Avenue, St. Paul, MN 55108, United States. Fax: +1 612 625 5780.

PII: S0014-5793(07)00115-9

doi:10.1016/j.febslet.2007.01.068

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