Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: Evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin

Journal of Biological Inorganic Chemistry

Volumn 4, Issue 1, 1999, Pages 56-63

  Rompel, Annette ^a   Fischer, Helmut ^a   Meiwes, Dirk ^a   Büldt Karentzopoulos, Klaudia ^a   Dillinger, Renée ^b   Tuczek, Felix ^b   Witzel, Herbert ^a   Krebs, Bernt ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Hemocyanin; Metalloprotein; Oxygen binding; Type 3 copper center; Tyrosinase

Indexed keywords

CATECHOL; CATECHOL OXIDASE; COPPER; HEMOCYANIN; HYDROGEN PEROXIDE; METALLOPROTEIN; MONOPHENOL MONOOXYGENASE; OXYGEN;

ARTHROPOD; ARTICLE; ATOMIC ABSORPTION SPECTROMETRY; ELECTRON SPIN RESONANCE; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL; RAMAN SPECTROMETRY;

BINDING SITES; CATECHOL OXIDASE; CATECHOLS; COPPER; CYANIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME INHIBITORS; HEMOCYANIN; HYDROGEN-ION CONCENTRATION; MOLECULAR WEIGHT; MONOPHENOL MONOOXYGENASE; PHENYLTHIOUREA; PLANTS; SPECTROPHOTOMETRY, ATOMIC; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN; TREES;

ARTHROPODA; LYCOPUS; LYCOPUS EUROPAEUS; OXY; POPULUS; POPULUS NIGRA;

EID: 0032941536     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007750050289     Document Type: Article

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