Abstract
The complete amino acid sequence of cytochrome c-552 from an extremely thermophilic hydrogen bacterium, Hydrogenobacter thermophilus TK-6 (IAM 12695), was determined. It is a single polypeptide chain of 80 residues, and its molecular weight, including heme, was calculated to be 7,599. The sequence of cytochrome c-552 from H. thermophilus TK-6 closely resembles that of cytochromes c-551 from Pseudomonas species. Moreover, the tertiary structure of Hydrogenobacter cytochrome c-552 is suggested to be similar to that of cytochrome c-551 from Pseudomonas aeruginosa. The sequence similarity between Hydrogenobacter cytochrome c-552 and that of other bacteria physiologically related to H. thermophilus is not high.
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Selected References
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- Almassy R. J., Dickerson R. E. Pseudomonas cytochrome c551 at 2.0 A resolution: enlargement of the cytochrome c family. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2674–2678. doi: 10.1073/pnas.75.6.2674. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ambler R. P., Meyer T. E., Trudinger P. A., Kamen M. D. The amino acid sequence of the cytochrome c-554(547) from the chemolithotrophic bacterium Thiobacillus neapolitanus. Biochem J. 1985 May 1;227(3):1009–1013. doi: 10.1042/bj2271009. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bowien B., Schlegel H. G. Physiology and biochemistry of aerobic hydrogen-oxidizing bacteria. Annu Rev Microbiol. 1981;35:405–452. doi: 10.1146/annurev.mi.35.100181.002201. [DOI] [PubMed] [Google Scholar]
- CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
- Chou P. Y., Fasman G. D. Empirical predictions of protein conformation. Annu Rev Biochem. 1978;47:251–276. doi: 10.1146/annurev.bi.47.070178.001343. [DOI] [PubMed] [Google Scholar]
- Dickerson R. E. Cytochrome c and the evolution of energy metabolism. Sci Am. 1980 Mar;242(3):137–153. [PubMed] [Google Scholar]
- Evans M. C., Buchanan B. B., Arnon D. I. A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc Natl Acad Sci U S A. 1966 Apr;55(4):928–934. doi: 10.1073/pnas.55.4.928. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HORIO T., HIGASHI T., SASAGAWA M., KUSAI K., NAKAI M., OKUNUKI K. Preparation of crystalline Pseudomonas cvtochrome c-551 and its general properties. Biochem J. 1960 Oct;77:194–201. doi: 10.1042/bj0770194. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hon-nami K., Oshima T. Cytochrome oxidase from an extreme thermophile. Thermus thermophilus HB8. Biochem Biophys Res Commun. 1980 Feb 12;92(3):1023–1029. doi: 10.1016/0006-291x(80)90804-9. [DOI] [PubMed] [Google Scholar]
- Ishii M., Kawasumi T., Igarashi Y., Kodama T., Minoda Y. 2-Methylthio-1,4-naphthoquinone, a unique sulfur-containing quinone from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus. J Bacteriol. 1987 Jun;169(6):2380–2384. doi: 10.1128/jb.169.6.2380-2384.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller D. J., Nicholas D. J. N-terminal amino acid sequence of cytochrome c-552 from Nitrosomonas europaea. Biochem Int. 1986 Jan;12(1):167–172. [PubMed] [Google Scholar]
- Tanaka Y., Fukumori Y., Yamanaka T. The complete amino acid sequence of Nitrobacter agilis cytochrome c-550. Biochim Biophys Acta. 1982 Sep 22;707(1):14–20. doi: 10.1016/0167-4838(82)90390-9. [DOI] [PubMed] [Google Scholar]
- Van Beeumen J., Ambler R. P., Meyer T. E., Kamen M. O., Olson J. M., Shaw E. K. The amino acid sequences of the cytochromes c-555 from two green sulphur bacteria of the genus Chlorobium. Biochem J. 1976 Dec 1;159(3):757–769. doi: 10.1042/bj1590757. [DOI] [PMC free article] [PubMed] [Google Scholar]