Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein

Journal of Biological Chemistry

Volumn 280, Issue 9, 2005, Pages 7671-7676

  Yang, Jianhua ^a   Ishimori, Koichiro ^b   O'Brian, Mark R ^a  

^a UNIVERSITY AT BUFFALO   (United States)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DEGRADATION; IRON; PURIFICATION; REDOX REACTIONS; STRAIN; SUBSTITUTION REACTIONS;

HEME REGULATORY MOTIF (HRM); IRON RESPONSE REGULATOR (IRR); MUTANT STRAIN; REDOX STATES;

PROTEINS;

ALANINE; BACTERIAL PROTEIN; GLUTATHIONE TRANSFERASE; HEME; HISTIDINE; HYBRID PROTEIN; IRON; IRON RESPONSE REGULATOR PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; BRADYRHIZOBIUM JAPONICUM; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN MOTIF; PROTEIN PURIFICATION; SPECTROSCOPY; WILD TYPE;

ALANINE; AMINO ACID MOTIFS; BACTERIAL PROTEINS; BINDING SITES; BRADYRHIZOBIUM; FERROCHELATASE; GLUTATHIONE TRANSFERASE; HEME; HISTIDINE; IRON; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; OXYGEN; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; TIME FACTORS; TRANSCRIPTION FACTORS;

EID: 14844355242     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M411664200     Document Type: Article

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