Heinz Decker

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Heinz Decker (born November 27, 1950 in Regensburg ; † December 9, 2018 in Mainz ) was a biophysicist and university professor for molecular biophysics at Johannes Gutenberg University Mainz . He was known for his work in the fields of hemocyanins and tyrosinases .

Life

Heinz Decker studied biology and physics at the Ludwig Maximilians University in Munich (LMU) from 1971 to 1976 . There he was awarded a Dr. rer. nat doctorate . From 1982 to 1984 he worked abroad at the Department of Chemistry and Biochemistry at the University of Colorado, Boulder , USA, and as a Research Assistant Professor at the School of Medicine, Saint Louis University , Missouri, USA. 1984–85 Decker was a research assistant at the Max Planck Institute for Medical Research , Biophysics Department , Heidelberg and from 1985 to 1994 project manager for Molecular Physiology and Biophysics. In 1989 Decker completed his habilitation at the LMU Munich and was appointed senior research assistant in 1991. In 1993 he was a substitute professor at the Institute for Zoology at the University of Veterinary Medicine in Hanover . In 1994 he was also visiting professor at the Institute of Biology at the University of Padua , Italy. At the end of 1994 Decker accepted an appointment as C4 professor for molecular biophysics at the Johannes Gutenberg University in Mainz, where he has headed the institute of the same name since then. Decker took a research semester in 1998 at the Oregon Institute of Marine Biology, University of Oregon , at the University of Padua, Italy and in 2006 at the Marine Biology Laboratory Woods Hole, Massachusetts, USA.

Decker was a founding member of the Mainz Wine Senate and the Rotary Club Mainz-Rheinhessen.

Scientific contribution

Decker's research interests were in the role of oxygen in the evolution of life. To this end, he examined the structure, function and evolution of type 3 copper proteins and their nanotechnological and immunological application. Two groups of proteins are of particular importance: a) the oxygen transport through hemocyanins in arthropods (crabs, spiders, scorpions etc.) and mollusks (snails, mussels etc.), b) the enzymes tyrosinase and catechol oxidases , which are found in all organisms from bacteria to Humans and have different biological functions. They start the synthesis of melanin , which is responsible for the coloring of our hair and skin, but also for the brown coloring of fruits, plants, mushrooms and animal organisms. Decker draws particular attention with his ideas about the mechanism of graying hair or albinism. In addition, melanin is often part of the immune response against pathogenic intruders or helps to close wounds. Hemocyanins can also be converted to tyrosinases and catecholases . Decker made important contributions to the molecular mechanisms of activation and catalysis of this type 3 copper protein family. To do this, he made use of various biophysical methods.

In order to understand the interaction of up to 160 oxygen binding centers, Decker worked during his time at Stanley Gill (Boulder, Colorado) on the nesting model, which assigns allosteric equilibria to hierarchies in the structure of cooperative protein complexes and thus also the function of other protein complexes such as extracellular ones Hemoglobins "and GroEL .

A recent focus is the education of wine proteins with regard to their potential for intolerance reactions and allergies as well as their importance for the formation of turbidity .

Together with Wolfgang Weuffen, a book about thiocyanate was created .

Research projects

Since 2002, Decker has been involved in several special research projects, graduate colleges and individual projects of the German Research Foundation , in projects of the BMBF , in a working group of the BMWi , in projects of the European Cooperation in Science and Technology (COST) and those of the Rhineland-Palatinate Foundation for Innovation.

Memberships in scientific associations

Publications

Books

  • with W. Weuffen (Ed.): Thiocyanate - a bioactive ion with an orthomolecular character. ISMH Verlag, Sarow 2004, ISBN 3-934043-06-2 .
  • with K. van Holde: Oxygen and the Evolution of Life. 1st edition. Springer Verlag, Heidelberg / Berlin 2011, ISBN 978-3-642-13178-3 .
  • with H. König: Vine and wine as a cultural asset. 1st edition. Spektrum Akademischer Verlag, Heidelberg 2013, ISBN 978-3-8274-2886-8 .

items

Web links

Individual evidence

  1. ↑ https://www.vrm-trauer.de/trauerbeispiel/heinz-decker
  2. ↑ Mainz Wine Senate
  3. ^ H. Decker, K. van Holde: Oxygen and the Evolution of Life. 1. Aage. Springer Verlag, Heidelberg / Berlin 2011, ISBN 978-3-642-13178-3 .
  4. ↑ J. Markl, H. Decker: Molecular structure of arthropodan hemocyanins. In: Advances in Comparative and Environmental Physiology. 13, 1992, pp. 325-376.
  5. ↑ K. van Holde, KI Miller; H. Decker: Hemocyanin and invertebrate evolution. In: J Biol Chem 276, 2001, pp. 15563-15566.
  6. ↑ H. Decker, T. Rimke: Two different functions of one active site: Binding oxygen and phenoloxidase activity of hemocyanin of tarantula hemocyanin. In: J.Biol. Chem. 273, 1998, pp. 25889-25892.
  7. ↑ JM Wood, H. Decker, H. Hartmann, B. Chavan, H. Rokos, JD Spencer, S. Hasse, J. Thornton, M. Shalbaf, R. Paus, KU Schallreuter: Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair. In: FASEB J . 23, 2009, pp. 2065-2075.
  8. ^ T. Schweikardt, C. Olivares, F. Solano, E. Jaenicke, JC Garcia-Borron, H. Decker: A 3D model of mammalian tyrosinase active site accounting for loss of function mutations. In: Pigment Cell Research . 20, 2007, pp. 394-401.
  9. ^ M. Rolff, J. Schottenheim, H. Decker, F. Tuczek: Copper-O2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. In: Chemical Society Reviews. 40, 2011, pp. 4077-4098.
  10. ^ H. Decker, T. Schweikardt, F. Tuczek: The first crystal structure of tyrosinase: all questions answered? In: Angewandte Chemie. Engl Ed., 45, 2006, pp. 4546-4550.
  11. ^ H. Decker, R. Dillinger, F. Tuczek: How does tyrosinase work? Recent insights from model chemistry and structural biology. In: Angewandte Chemie. Int. Ed. 39, 2000, pp. 1587-1591.
  12. ^ H. Decker, F. Tuczek: Phenoloxidase activity of hemocyanins: Activation, substrate orientation and molecular mechanism. In: Trends in Biochem. Sci. 25, 2000, pp. 392-397.
  13. ^ H. Hartmann, A. Bongers, H. Decker: Monte Carlo based reconstruction of keyhole limpet hemocyanin type 1 (KLH1): Small angle X-ray scattering reveals oxygen dependent conformational change of the surface. In: J. Biol. Chem. 279, 2004, pp. 2841-2845.
  14. ↑ M. Lippitz, W. Erker, H. Decker, K. van Holde, T. Basche: Two-photon spectroscopy and microscopy of tryptophan containing single proteins. In: Proc. Natl. Acad. Sci. USA 99, 2002, pp. 2772-2777.
  15. ↑ E. Jaenicke, B. Pairet, H. Hartmann, H. Decker: Crystallization and preliminary analysis of crystals of the 24-meric hemocyanin of the emperor scorpion (Pandinus imperator). In: PLoS One. 2012; 7 (3), p. E32548. Epub 2012 Mar 5
  16. ↑ Y. Cong, SJ Ludtke, DSA Woolford, HA Khant, W. Chiu, T. Schweikardt, H. Decker: SDS induced conformational change of scorpion hemocyanin as revealed by electron cryo-microscopy at 8 Å resolution. In: Structure. 17, 2009, pp. 749-758.
  17. ^ CH Robert, H. Decker, B. Richey, SJ Gill, J. Wyman: Nesting: Hierarchies of allosteric interactions. In: Proc. Natl. Acad. Sci. (USA) 84, 1987, pp. 1891-1895.
  18. ^ H. Decker, R. Sterner: Nested allostery of Arthropodan hemocyanin (Eurypelma californicum and Homarus americanus): The role of the protons. In: J. Mol. Biol. 211, 1990, pp. 281-293.
  19. ^ R. Sterner, H. Decker: Inversion of the Bohr effect during oxygen binding to a giant tarantula hemocyanin. In: Proc. Natl. Acad. Sci. USA 91, 1994, pp. 4835-4839.
  20. ↑ N. Hellmann, R. Weber, H. Decker: Nested allosteric interactions in extracellular hemoglobin of the leech Macrobdella decora. In: J. Biol. Chem. 278, 2003, pp. 44355-44360.
  21. ↑ N. Hellmann, H. Decker: Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in binding. In: BBA - Proteins and Proteomics. 1599, 2002, pp. 45-55.
  22. ↑ P. Wigand, M. Blettner, J. Saloga, H. Decker: Prevalence of wine intolerance: results of a survey from Mainz, Germany. In: Dtsches Ärztebl. Intl. 109, 2012, pp. 437-444.
  23. ↑ P. Fronk, M. Blettner, H. Decker: Self-reported consumption of wine and other alcoholic beverages in a German wine area. In: Intl J. Wine Research. 5, 2013, pp. 27-37.
  24. ↑ H. König, H. Decker (Ed.): Kulturgut Rebe und Wein. 1st edition. Spektrum Akademischer Verlag, Heidelberg 2012, ISBN 978-3-8274-2886-8 .
  25. ↑ W. Weuffen, H. Decker (Ed.): Thiocyanate - a bioactive ion with an orthomolecular character. ISMH Verlag, Sarow 2004, ISBN 3-934043-06-2 .
personal data
SURNAME Decker, Heinz
BRIEF DESCRIPTION German biophysicist
DATE OF BIRTH November 27, 1950
PLACE OF BIRTH regensburg
DATE OF DEATH December 9, 2018
Place of death Mainz