Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: Effect of Met95 mutations

Biochemical and Biophysical Research Communications

Volumn 299, Issue 2, 2002, Pages 169-172

  Watanabe, Miki ^a   Matsui, Toshitaka ^a   Sasakura, Yukie ^a   Sagami, Ikuko ^a   Shimizu, Toru ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

Axial ligand; Cyanide; Heme sensor; Optical absorption; Phosphodiesterase; Site directed mutagenesis

Indexed keywords

ALANINE; BACTERIAL ENZYME; CYANIDE; FERRIC ION; HISTAMINE; LEUCINE; LIGAND; PHOSPHODIESTERASE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CHEMICAL BINDING; CONTROLLED STUDY; DISSOCIATION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

AZIDES; CYANIDES; ESCHERICHIA COLI; FLUORIDES; HEME; IMIDAZOLES; IRON; KINETICS; METHIONINE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHORIC DIESTER HYDROLASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY;

ESCHERICHIA COLI;

EID: 0036436657     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02621-9     Document Type: Article

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