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pro vyhledávání: '"551"'
Publikováno v:
Biochemistry. 50(12)
Hyperthermophilic Aquifex aeolicus cytochrome c(555) (AA c(555)) exceptionally folds even in the apo state, unlike general cytochromes c including mesophilic Pseudomonas aeruginosa cytochrome c(551) (PA c(551)), which is structurally homologous to AA
Publikováno v:
Biochemistry. 48:8062-8069
The thermodynamic properties of the redox potentials (E(m)) of Pseudomonas aeruginosa cytochrome c(551) (PA) and its mutants possessing a variety of pK(a) values for the heme 17-propionic acid side chain, which ranged from approximately 5 to approxim
Autor:
Jun Hasegawa, Yoshihiro Sambongi, Hajime Mita, Shin-ichi Mikami, Shin-ichi J. Takayama, Yasuhiko Yamamoto, Norifumi Terui
Publikováno v:
Biochemistry. 44:5488-5494
Pseudomonas aeruginosa cytochrome c(551) and a series of its mutants exhibiting various thermostabilities have been studied by paramagnetic (1)H NMR and cyclic voltammetry in an effort to elucidate the molecular mechanisms responsible for control of