Stabilization mechanism of cytochrome c552 from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 8, 2008, Pages 2103-2109

  Hakamada, Sayaka ^a   Sonoyama, Takafumi ^a   Ichiki, Shin Ichi ^a   Nakamura, Shota ^b,c   Uchiyama, Susumu ^b   Kobayashi, Yuji ^b,d   Sambongi, Yoshihiro ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

Cytochrome c; Electrostatic interaction; Protein stability; Site directed mutagenesis

Indexed keywords

CYTOCHROME C; ELECTROSTATIC INTERACTION; PROTEIN STABILITY; SITE-DIRECTED MUTAGENESIS;

CYTOCHROME C; CYTOCHROME C-552; CYTOCHROME C552;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRICITY; ENZYMOLOGY; GENETICS; HYDROGENOPHILACEAE; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; TEMPERATURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CYTOCHROME C GROUP; ELECTROSTATICS; HYDROGENOPHILACEAE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); HYDROGENOBACTER THERMOPHILUS; HYDROGENOPHILUS THERMOLUTEOLUS; PSEUDOMONAS AERUGINOSA;

EID: 50649103330     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80187     Document Type: Article

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