A new soluble 10kDa monoheme cytochrome c-552 from the anammox bacterium Candidatus "Kuenenia stuttgartiensis"

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 10kDa soluble cy...

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Bibliographic Details
Published in:FEMS microbiology letters 2005-11, Vol.252 (2), p.273-278
Main Authors: Cirpus, Irina E Y, de Been, Mark, den Camp, Huub J M Op, Strous, Marc, Le Paslier, Denis, Kuenen, Gijs J, Jetten, Mike S M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteria, Anaerobic - chemistry
Bacteria, Anaerobic - genetics
Chromatography, Ion Exchange
Cytochromes c - chemistry
Cytochromes c - genetics
Cytochromes c - isolation & purification
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
Electrophoresis, Polyacrylamide Gel
Geobacter - genetics
Geobacter sulfurreducens
Heme - analysis
Molecular Sequence Data
Molecular Weight
Nitrosomonas europaea
Nitrosomonas europaea - genetics
Sequence Analysis, DNA
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Solubility
Spectrum Analysis
Ultracentrifugation
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Summary: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 10kDa soluble cytochrome c was purified from cell extracts using ultracentrifugation and anion exchange chromatography. The UV/Vis spectrum of the reduced cytochrome showed the gamma, beta and alpha absorption maxima at 419, 522 and 552nm, 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.
ISSN:0378-1097
DOI:10.1016/j.femsle.2005.09.007