Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase

Biochemical and Biophysical Research Communications

Volumn 450, Issue 1, 2014, Pages 767-772

  Morishita, Hirotoshi ^a   Kurita, Daisuke ^a   Kataoka, Kunishige ^a   Sakurai, Takeshi ^a  

^a KANAZAWA UNIVERSITY   (Japan)

Author keywords

Bilirubin oxidase; Dioxygen reduction; Hydrogen bond network; Multicopper oxidase

Indexed keywords

ALANINE; BILIRUBIN OXIDASE; COPPER; CYSTEINE; GLUTAMIC ACID; GLUTAMINE; MUTANT PROTEIN; OXIDOREDUCTASE; OXYGEN; PEROXIDE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; HYDROGEN BOND; MUTATION; PRIORITY JOURNAL; PROTON TRANSPORT; REDUCTION; SIGNAL TRANSDUCTION;

BILIRUBIN OXIDASE; DIOXYGEN REDUCTION; HYDROGEN BOND NETWORK; MULTICOPPER OXIDASE;

BINDING SITES; COPPER; ENZYME ACTIVATION; GLUTAMIC ACID; HYDROGEN; HYDROGEN BONDING; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXIDOREDUCTASES ACTING ON CH-CH GROUP DONORS; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP; WATER;

EID: 84907210802     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.06.052     Document Type: Article

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