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Article

Five amino acid residues responsible for the high stability of Hydrogenobacter thermophilus cytochrome c552: reciprocal mutation analysis.

The Journal of biological chemistry - 18 Feb 2005

Oikawa Kenta, Nakamura Shota, Sonoyama Takafumi, Ohshima Atsushi, Kobayashi Yuji, Takayama Shin-ichi J, Yamamoto Yasuhiko, Uchiyama Susumu, Hasegawa Jun, Sambongi Yoshihiro

Abstract excerpt

Five amino acid residues responsible for extreme stability have been identified in cytochrome c(552) (HT c(552)) from a thermophilic bacterium, Hydrogenobacter thermophilus. The five residues, which are spatially distributed in three regions of HT c(552), were replaced with the corresponding residues in the homologous but less stable cytochrome c(551) (PA c(551)) from Pseudomonas aeruginosa. The quintuple HT...

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PMID: 15598654
DOI: 10.1074/jbc.M412392200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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