Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: Direct evidence for ligation of two histidines in the copper(II)- reconstituted protein

Biochemistry

Volumn 38, Issue 34, 1999, Pages 11062-11072

  Coulter, Eric D ^a,c   Moon, Namdoo ^b   Batie, Christopher J ^a,d   Dunham, William R ^a   Ballou, David P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c UNIVERSITY OF GEORGIA   (United States)

^d NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; COPPER; FERROUS ION; HISTIDINE; MANGANESE; METAL ION; OXYGENASE; PHTHALATE DIOXYGENASE; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; METAL BINDING; MOLECULAR INTERACTION; OXYGENATION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

APOENZYMES; BINDING SITES; BURKHOLDERIA CEPACIA; CATIONS, DIVALENT; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX III; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HISTIDINE; IRON-SULFUR PROTEINS; MULTIENZYME COMPLEXES; OXIDATION-REDUCTION; OXYGENASES; SPECTROPHOTOMETRY, ULTRAVIOLET; TYROSINE;

EID: 0033600552     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9904499     Document Type: Article

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