An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77 K: The effects of component interactions and the binding of small molecules to the diiron(III) center

Biochemistry

Volumn 38, Issue 13, 1999, Pages 4188-4197

  Davydov, Roman ^a,b   Valentine, Ann M ^b   Komar Panicucci, Sonja ^b   Hoffman, Brian M ^a   Lippard, Stephen J ^b  

^a NORTHWESTERN UNIVERSITY   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IRON; METHANE MONOOXYGENASE;

ARTICLE; BINDING SITE; COMPLEX FORMATION; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; LIGAND BINDING; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; THERMOSTABILITY;

BINDING SITES; DIMETHYL SULFOXIDE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRONS; FERRIC COMPOUNDS; FERROUS COMPOUNDS; FREEZING; METHYLOCOCCACEAE; OXIDATION-REDUCTION; OXYGENASES; PHENOLS; SOLUBILITY;

EID: 0033616807     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982391o     Document Type: Article

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