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The amino acid sequence of rusticyanin isolated from Thiobacillus ferrooxidans
Author(s) -
Yano Takahiro,
Fukumori Yoshihiro,
Yamanaka Tateo
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81025-4
Subject(s) - thiobacillus ferrooxidans , chemistry , biochemistry , sequence (biology) , peptide sequence , thiobacillus , microbiology and biotechnology , biology , gene , ferrous , organic chemistry , sulfur
The amino acid sequence of rusticyanin, a copper protein, purified from the iron‐oxidizing bacterium Thiobacillus ferrooxidans was determined. Rusticyanin contained 154 amino acid residues in a single polypeptide chain and its molecular weight was calculated to be about 16400 based on the amino acid sequence. The N‐terminal sequence up to the 20th residue of the protein apparently resembled those of Methylobacterium extorquens AMI amicyanin and poplar leaf plastocyanin rather than those of azurin family proteins. In the C‐terminal region of the sequence, rusticyanin had one cysteine, one histidine and one methionine which are conserved through many copper proteins. In the middle region of the sequence, rusticyanin was not similar to any other copper protein. The sequence nearby His 84 of rusticyanin was similar to those of other copper proteins to some extent. However, Asn which follows His 84 and is highly conserved in other copper proteins did not exist in rusticyanin. Therefore, it seemed difficult to conclude on the basis of the results obtained in the present study that His 84 in rusticyanin was the fourth ligand to the copper atom.