Abstract
The composition of membrane-bound electron-transferring proteins from denitrifying cells of Haloarcula marismortui was compared with that from the aerobic cells. Accompanying nitrate reductase catalytic NarGH subcomplex, cytochrome b-561, cytochrome b-552, and halocyanin-like blue copper protein were induced under denitrifying conditions. Cytochrome b-561 was purified to homogeneity and was shown to be composed of a polypeptide with a molecular mass of 40 kDa. The cytochrome was autooxidizable and its redox potential was −27 mV. The N-terminal sequence of the cytochrome was identical to the deduced amino acid sequence of the narC gene product encoded in the third ORF of the nitrate reductase operon with a unique arrangement of ORFs. The sequence of the cytochrome was homologous with that of the cytochrome b subunit of respiratory cytochrome bc. A possibility that the cytochrome bc and the NarGH constructed a supercomplex was discussed.
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Acknowledgments
We would like to thank Prof. Dr. Y. Fukumori (Department of Biology, Kanazawa University) and Prof. Dr. T. Sakurai (Department of Chemistry, Kanazawa University) for the low-temperature spectroscopic measurement and cyclic voltammetric analysis, respectively. This work was supported in part by Grant 0322 from the Salt Science Research Foundation and in part by Grant-In-Aid 15019037 from the Ministry of Education, Science, Sports and Culture, Japan (to T.F.).
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Communicated by K. Horikoshi
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Yoshimatsu, K., Araya, O. & Fujiwara, T. Haloarcula marismortui cytochrome b-561 is encoded by the narC gene in the dissimilatory nitrate reductase operon. Extremophiles 11, 41–47 (2007). https://doi.org/10.1007/s00792-006-0016-3
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DOI: https://doi.org/10.1007/s00792-006-0016-3