Substitutions of the "bridging" aspartate 178 result in profound changes in the reactivity of the Rieske center of phthalate dioxygenase

Biochemistry

Volumn 45, Issue 30, 2006, Pages 9032-9041

  Pinto, Alex ^a   Tarasev, Michael ^a   Ballou, David P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; HYDROXYLATION; IRON COMPOUNDS; MOLECULAR ORIENTATION; OXIDATION; SUBSTITUTION REACTIONS;

FERROUS IONS; INTRAMOLECULAR ELECTRON TRANSFER; PHTHALATE DIOXYGENASE (PDO); RIESKE DIOXYGENASES;

ENZYMES;

ALANINE; ASPARAGINE; ASPARTIC ACID; DIOXYGENASE; FERROUS ION; IRON; MUTANT PROTEIN; OXIDOREDUCTASE; PHTHALATE DIOXYGENASE; PHTHALATE REDUCTASE; PHTHALIC ACID; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; DISSOCIATION CONSTANT; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME METABOLISM; HYDROXYLATION; OXIDATION; PRIORITY JOURNAL; REDUCTION;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; BURKHOLDERIA CEPACIA; CATALYSIS; ELECTRON TRANSPORT COMPLEX III; HYDROXYLATION; IRON-SULFUR PROTEINS; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGENASES; PHTHALIC ACIDS;

EID: 33746640863     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060216z     Document Type: Article

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