| Literature DB >> 7767224 |
T Fujiwara1, T Yamanaka, Y Fukumori.
Abstract
The complete amino acid sequence of cytochrome c-552 derived from the chemoautotrophic ammonia-oxidizing bacterium Nitrosomonas europaea was determined. The cytochrome consisted of 81 amino acid residues, and its molecular weight was calculated to be 9098 including heme c. Although the sequence of cytochrome c-552 was highly homologous to those of cytochromes c-551, which were known as the electron-donating components to dissimilatory nitrite reductase in pseudomonads, cytochrome c-552 differed from cytochrome c-551 in two points: (1) the sequence of cytochrome c-552 was shorter by two amino acid residues than that of cytochrome c-551 at the N-terminus and (2) one amino acid insertion was present in cytochrome c-552.Entities:
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Year: 1995 PMID: 7767224 DOI: 10.1007/BF00294624
Source DB: PubMed Journal: Curr Microbiol ISSN: 0343-8651 Impact factor: 2.188