The amino acid sequence of rusticyanin isolated from Thiobacillus ferrooxidans

FEBS Letters

Yamanaka, Tateo¹  Fukumori, Yoshihiro¹  Yano, Takahiro¹ 

[1] Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Yokohama, 227, Japan

关键词: Thiobacillus ferrooxidans;    Amino acid sequence;    Rusticyanin;    Copper protein;   

DOI  :  10.1016/0014-5793(91)81025-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 His⁸⁴ of rusticyanin was similar to those of other copper proteins to some extent. However, Asn which follows His⁸⁴ 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 His⁸⁴ in rusticyanin was the fourth ligand to the copper atom.

【 授权许可】

Unknown