In meso crystal structure of a novel membrane-associated octaheme cytochrome c from the Crenarchaeon Ignicoccus hospitalis

Author:

Parey Kristian1,Fielding Alistair J.2,Sörgel Matthias3,Rachel Reinhard4,Huber Harald4,Ziegler Christine5,Rajendran Chitra5

Affiliation:

1. Department of Structural Biology; Max Planck Institute of Biophysics; Frankfurt am Main Germany

2. School of Chemistry and the Photon Science Institute; University of Manchester; UK

3. Biogeochemistry Department; Max Planck Institute for Chemistry; Mainz Germany

4. Department of Microbiology; University of Regensburg; Germany

5. Department of Structural Biology; University of Regensburg; Germany

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference51 articles.

1. Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling;Simon;Biochem Soc Trans,2011

2. Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations;Simon;Biochim Biophys Acta,2013

3. Characterization of hydroxylamine-cytochrome c reductase from the chemoautotrophs Nitrosomonas europaea and Nitrosocystis oceanus;Hooper;J Biol Chem,1965

4. Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species;Tikhonova;FEBS J,2012

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