H
Herbert Witzel
Researcher at University of Münster
Publications - 44
Citations - 1916
Herbert Witzel is an academic researcher from University of Münster. The author has contributed to research in topics: Purple acid phosphatases & Acid phosphatase. The author has an hindex of 20, co-authored 44 publications receiving 1890 citations.
Papers
More filters
Journal ArticleDOI
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.
TL;DR: 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.
Journal ArticleDOI
Mechanism of Fe III –Zn II purple acid phosphatase based on crystal structures
TL;DR: 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.
Journal ArticleDOI
Diadenosine phosphates and the physiological control of blood pressure
Hartmut Schlüter,Elmar Offers,Gitte Brüggemann,Marcus van der Giet,Martin Tepel,Eckhard Nordhoff,Michael Karas,Claus Spieker,Herbert Witzel,Walter Zidek +9 more
TL;DR: It is concluded that AP5A and AP6A may play a part in local vasoregulation and possibly in the regulation of blood pressure.
Journal ArticleDOI
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.
Annette Rompel,Helmut Fischer,Dirk Meiwes,Klaudia Büldt-Karentzopoulos,Renée Dillinger,Felix Tuczek,Herbert Witzel,Bernt Krebs +7 more
TL;DR: 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.
Journal ArticleDOI
Structural relationship between the mammalian Fe(III)Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatases
TL;DR: Primary structure predictions indicate that Uf contains two βαβαβ motifs thus resembling the folding topology of the plant enzyme, and a tentative model for the mammalian PAP can be constructed.