Crystal structure of a plant catechol oxidase containing a dicopper center
- T. Klabunde, C. Eicken, J. Sacchettini, B. Krebs
- ChemistryNature Structural Biology
- 1 December 1998
Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB ofThe oxygenated enzyme.
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures.
- T. Klabunde, N. Sträter, R. Fröhlich, H. Witzel, B. Krebs
- ChemistryJournal of Molecular Biology
- 21 June 1996
All three structures reported herein support a mechanism of phosphate ester hydrolysis involving interaction of the substrate with Zn(II) followed by a nucleophilic attack on the phosphorus by an Fe(III)-coordinated hydroxide ion.
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.
- N. Sträter, T. Klabunde, P. Tucker, H. Witzel, B. Krebs
- ChemistryScience
- 9 June 1995
The active-site structure of the homodimeric 111-kilodalton KBPAP is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion.
The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins.
- C. Gerdemann, C. Eicken, B. Krebs
- BiologyAccounts of Chemical Research
- 7 February 2002
Comparison between the 3D structures of catechol oxidase and hemocyanins reveals the structural reasons for the divergence in function.
Oxidative switches in functioning of mammalian copper chaperone Cox17.
- A. Voronova, W. Meyer‐Klaucke, P. Palumaa
- BiologyBiochemical Journal
- 15 November 2007
XAS (X-ray absorption spectroscopy) determined that Cu4Cox17 contains a Cu4S6-type copper-thiolate cluster, which may provide safe storage of an excess of copper ions.
Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type‐3 dicopper center 1
- C. Eicken, F. Zippel, K. Büldt-Karentzopoulos, B. Krebs
- PhysicsFEBS Letters
- 2 October 1998
Catechol oxidase - structure and activity.
- C. Eicken, B. Krebs, J. Sacchettini
- BiologyCurrent Opinion in Structural Biology
- 1 December 1999
Matrix‐assisted laser desorption/ionization mass spectrometry with additives to 2,5‐dihydroxybenzoic acid
Selected benzoic acid derivatives and related substances were used as additives to 2,5-dihydroxybenzoic acid (2,5 DHB) and the performance of the mixtures in matrix-assisted laser…
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…
- A. Rompel, H. Fischer, B. Krebs
- Chemistry, BiologyJBIC Journal of Biological Inorganic Chemistry
- 1 February 1999
The intense resonance Raman peak at 277 cm–1, belonging to a Cu-N (axial His) stretching mode, suggests that catechol oxidase has six terminal His ligands, as known for molluscan and arthropodan hemocyanin.
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