| Literature DB >> 12296704 |
Yasuhiko Yamamoto1, Norifumi Terui, Naoki Tachiiri, Kazuhisa Minakawa, Hitomi Matsuo, Tsunenori Kameda, Jun Hasegawa, Yoshihiro Sambongi, Susumu Uchiyama, Yuji Kobayashi, Yasuo Igarashi.
Abstract
Paramagnetic NMR and optical studies of the oxidized forms of mesophile Pseudomonas aeruginosa cytochrome c(551) and its quintuple mutant (F7A/V13M/F34Y/E43Y/V78I), and thermophile Hydrogenobacter thermophilus cytochrome c(552) demonstrated that the amino acid side chain packings in the protein interior influence the coordination bond between the heme iron and the axial methionine in the proteins. The strength of heme axial coordinations was found to correlate with the overall protein thermostability.Entities:
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Year: 2002 PMID: 12296704 DOI: 10.1021/ja025597s
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419