Open AccessA new soluble 10 kDa monoheme cytochrome c ‐552 from the anammox bacterium Candidatus “ Kuenenia stuttgartiensis ”
Author(s) -
Cirpus Irina E.Y.,
Been Mark,
Camp Huub J.M.,
Strous Marc,
Paslier Denis,
Kuenen Gijs J.,
Jetten Mike S.M.
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2005.09.007
Subject(s) - cytochrome , biochemistry , cytochrome c , nitrosomonas europaea , chemistry , bacteria , biology , nitrite , enzyme , genetics , organic chemistry , nitrate , mitochondrion
Abstract The chemolithoautotrophic anammox bacterium Candidatus “ Kuenenia stuttgartiensis ” grows anaerobically using ammonium as electron donor for nitrite reduction. More than 10% of the proteins in cell extracts of “ K. stuttgartiensis ” consist of c ‐type heme proteins. A 10 kDa soluble cytochrome c was purified from cell extracts using ultracentrifugation and anion exchange chromatography. The UV/Vis spectrum of the reduced cytochrome showed the γ, β and α absorption maxima at 419, 522 and 552 nm, respectively. The N‐terminal amino acid sequence and peptide fragments of the tryptic digest of the protein were used to identify the corresponding gene. Analysis of the gene product showed that the protein was preceded by a 30 amino acids long leader sequence and that it belonged to the low‐spin class ID cytochrome c . The CXXCH motive was located at the N‐terminal site of the protein. The gene organization of the cytochrome showed some resemblance to cytochrome c clusters of unknown function in the genome of Nitrosomonas europaea and Geobacter sulfurreducens PCA.