Univ.-Prof. Dr. Heinz Decker

Institut für Molekulare Biophysik
Johannes Gutenberg-Universität
Jakob Welder Weg 26
55128 Mainz
Deutschland

Tel: ++49-(0)6131-3923570
Fax: ++49-(0)6131-3923557
email:

 

[Education] - [Financing] - [Reviewing][Publications]

Education & Professional Experience

 since   1995

C4 Professor for Molecular Biophysics and
Head of the Institute, Johannes Gutenberg-
University Mainz

1993 - 1994

Commissioner of C4 Professor and Director of
the Institute of Zoology, Veterinary University
Hannover TiHo

1994

Visiting Professor, Institute of Biology,
University of Padova, Italy

 1989

Dr. habil (Habilitation and Venia Legendi),
LMU

 1985 - 1994

Project Leader for Molecular Physiology and
Biophysics, since 1991 as C2 at the Institute
of Biology, LMU

 1984 - 1985

Res. Associate, MPI for Medical Research,
Dept. for Biophysics, Heidelberg

1983 - 1984

Res. Assistant Professor, School of Medicine,
St. Louis University, MO, USA.

 1982 - 1983

Res. Associate, Dept. of Chem. & Biochem.,
Univ.of Colorado, Boulder, CO, USA.

 1981

Dr. rer. nat (LMU)

 1971 - 1976

Biology and Physics at the Ludwig Maximilians
University Munich (LMU), 1. Staatsexamen für
GymnasienStudium der Biologie und Physik

 

Financing
  • SFB 490: Invasion and Persistence at Infections  (Project D4, Hellmann, Decker, 2006-2011) Pore formation of alpha-toxin from S. aureus
  • SFB 625: From Single Molecules to Nanoscopic Structured Materials (Project B5, Decker, Markl, Schönhense 2002-Juni 2005) Surface bound hemocyanins
  • GRK 1043: International Graduate School of Immunotherapy (Project B2, 2004-2014) Comparison of crystal and solution structures of arthropod hemocyanins
  • De414/7-1 (Decker, Basché; 1999-2003) Einzelmolekülspektroskopie
  • De414/8-1,8-2 (Decker, 2002-2006) Phenoloxidaseaktivität von Hämocyaninen und Tyrosinasen
  • De414/12-1 (Decker, Schönhense 2005-2009) Ortsaufgelöste Röntgen-Nahkantenspektroskopie (XANES-PEEM) von Kupfer in Hämocyanin-Molekülen unter in-vivo-nahen Bedingungen
  • EU D21 COST:Molecular oxygen activation at biological and biomimetic metal centres (2001-2006)
  • EU COST CM1003: Biological oxidation reactions - mechanisms and design of newcatalysts. (2011-2014) WG2: Oxidation/Oxygenation of phenolic andrelated substrates, mainly by dicopper Systems
  • Stiftung Innovation Rheinland-Pfalz 929 (2010-2012)  Verträglichkeit von Wein: Weinproteine und ihr allergenes Potential
  • Stiftung Innovation Rheinland-Pfalz 1051 (2013-2015) Wirkung von oxidierenden Enzymen au die Farbe, sensorisch relevante und gesundheitsfördernde Inhaltsstoffe des Weines
  • BMBF Zentrum (2001-2003) Multifunktionelle Werkstoffe und miniaturisierte Funktionseinheiten: Koordinator Teilgruppe 4: Biosensoren (Decker), Projekt 4-1 (Decker): Nanosensor Hämocyanin
  • BMBF 05 KS7UMA (Langguth, Nawroth, Decker, Frey; 7/2007-6/2010, with extension to 6/2014):Indirekte Strahlentherapie IRT von Krebs mit Target-Nanopartikeln(http://foerderportal.bund.de/foekat/jsp/SucheAction.do?actionMode=view&fkz=05KS7UMA)
  • Forschungskreis der Ernährungsindustrie e.V. (FEI, BMWi) (Dietrich, Will, Wigand, Decker; 2011- 2014): Nachweis, Isolation und Charakterisierung nachtrübungsrelevanter Weinproteine sowie Verfahren zur Vermeidung von Eiweißtrübungen in Weinen und Traubensäften (http://www.fei-bonn.de/projekte/projekt_des_monats/aktuell)
  • Research Center for Immunology Mainz (Saloga, Decker, April 2009 – März 2012): Bedeutung der Affinität der allergenspezifischen IgE-Antikörper zum Allergen für die Schwere der klinischen Reaktion
  • NMFZ Naturwissenschaftlich-Medizinisches Forschungszentrum Mainz (Decker, Tenzer, Schild: 2011-2013): Labelfreie quantitative Proteomanalytik von Weinbeeren im Verlauf der Reifung und während der Weinbereitung

Reviewing

  • Biochemistry, Archives Biophysics and Biochemistry, Comp.Biochemistry and Biophysics, Biophysical J., Eur. J. Biochemistry, Biological Chemistry, Biochimica et Biophysica Acta (BBA - Proteins and Proteomics), Biochemical J., J Exp Biology, MACROMOLECULAR RAPID COMMUNICATIONS, J of Inorganic Chemistry, JACS; J. Biol. Chem., Structure, etc. 
  • Deutsche Forschungsgemeinschaft, Israelische Forschungsgemeinschaft, Health Research Board Ireland, Schweizerische Nationalfond, CNR-Italy, NSF USA, etc.
Selected Publications
  • Weichart A, Besemer A.S., Ip P., Koziollek-Drechsler I., Hellmann N., Decker H., Robertson J., Chakrabartty A., Behl C., Clement A.A. (2013) Wild-type Cu/Zn superoxide dismutase stabilizes mutant vatiants by heterodimerization. Neurobiology of Disease, 62C: 479-488
  • Leona B. Martin L.B., Nikodinovic-Runic J., Solano F, Hartmann H., Decker H., O’Connor K.E. (2013) Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches, Biotechnology & Bioengineering 110:1849–1857
  • Fronk P., Blettner M., Decker H. (2013) Self-reported consumption of wine and other alcoholic beverages in a German wine area, Int. J. Wine Research 5: 27–37
  • Jaeckels N., Tenzer S, Rosfa S, Schild HJ, Decker H., Wigand P. (2013) Purification and structural characterisation of lipid transfer protein isoform 4 from red wine and grapes, Food Chemistry 138: 263–269
  • Wigand P., Blettner M., Decker H (2012) Rot-, Rose- und Weinweinkonsum in einer deutschen Weinregion. Deutsche Lebensmittel-Rundschau 108: 467-470
  • Decker H. (2012) Ist er nun gesund oder nicht? Wein biologisch betrachtet. Forschung & Lehre 9/12: 710-711
  • Wigand P., Blettner M., Saloga J.. Decker H. (2012) Prevalence of wine intolerance: results of a survey from Mainz, Germany. Dtsches Ärztebl. Intl. 109: 437-444
  • Jaenicke E., Pairet B., Hartmann H., Decker H (2012) Crystallization and preliminary analysis of crystals from the 24-meric hemocyanin of emperor scorpion (Pandinus imperator) PLoS ONE 7(3): e32548. doi:10.1371
  • Rolff M., Schottenheim J., Decker H., Tuczek F. (2011) Copper-O2 Reactivity of Tyrosinase Models Towards External Monophenolic Substrates: Molecular Mechanism and Comparison with the Enzyme. Chemical Society Reviews 40:4077-4098
  • Jaenicke E, Büchler K, Decker H, Markl J, Bahrends T, Gunnar Schroeder (2011) The refined structure of functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) reveals disulfide bridges, IUBMB Life 63:183-7
  • Wigand P., Decker H. (2010) Proteine imWein – Nahrungsmittelallergie durch Wein? Act Dermatolog 36:1–5
  • Jaenicke E., Büchler K., Markl J., Decker H., Bahrends T. (2010) The structure of the cupredoxin-like domain in hemocyanins, Biochemical J. 426:373-378.
  • Mindykowski B, Jaenicke E, Tenzer S, Cirak S, Schweikardt T, Schild HJ, Decker H (2010): "Cockroach allergens Per a 3 are oligomers", Dev. Comp. Immunol. 34:722-733
  • Meesters C, Brack A, Hellmann N, Decker H (2009): "Structural Characterization of the α-Hemolysin Monomer from Staphylococcus aureus Proteins", Structure, Function and Bioinformatics 75:118-126
  • Wood JM, Decker H, Hartmann H, Chavan B, Rokos H, Spencer JD, Hasse S, Thornton J, Shalbaf M, Paus R, Schallreuter KU (2009): "Senile hair greying: H2O2-mediated oxidative stress affects human hair colour by blunting methionine sulfoxide repair", FASEB J. 23: 2065-2075
  • Cong Y, Ludtke SJ, Woolford DSA, Khant HA, Chiu W, Schweikardt T, Decker H (2009). "SDS induced conformational change of scorpion hemocyanin as revealed by electron cryo-microscopy at 8 Å resolution", Structure 17:749-758
  • Bellinghausen J, Häringer B, Lafargue B, Strand D, König B, Knop J, Decker H, Saloga J (2008): "Comparison of the immunogenicity and allergenicity of the monomeric and hexameric structure of the cockroach major allergen Per a 3", Clinical and Experimental Allergy 38:539-548
  • Nillius D, Jaenicke E, Decker H (2008): "Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin", FEBS Letters 582:749–754
  • Jaenicke E, Decker H (2008): "Kinetic properties of phenoloxidase-activity of tarantula hemocyanins", FEBS J 275: 1518-1528
  • Panzer D, Beck C, Maul J, Möller M, Decker H, Schönhense G (2008): "Transmission photoemission electron microscopy for lateral mapping of the X-ray absorption structure of a metalloprotein in a liquid cell", Eur. Biophys J 38:53-8
  • Pohlmann A, Möller M, Decker H, Schreiber WG (2007): "MRI of Tarantulas: morphologic and perfusion imaging at 1.5 Tesla", J Magnetic Resonance Imaging 25, 129-35
  • Schweikardt T, Olivares C, Solano F, Jaenicke E, Garcia-Borron JC, Decker H (2007): "A 3D model of mammalian tyrosinase active site accounting for loss of function mutations", Pigment Cell Research 20:394-401
  • Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F (2007): "Similar activation process and catalysis in hemocyanins and tyrosinases", Gene 398: 183-191
  • Decker H, Jaenicke E, Hellmann N, Lieb B, Meissner U, Markl J (2007): "Recent insights in the structure, function and evolution of hemocyanins", Integrative and Comparative Biology 47: 631-644
  • Baird S, Kelly SM, Price NC, Jaenicke E, Meesters C, Nillius D, Decker H, Nairn J (2007): "Hemocyanin conformational changes associated with SDS-induced phenol oxidase activation", Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1774:1380-1394
  • Claus H, Decker H (2006): "Bacterial Tyrosinases", Systematic and Applied Microbiology 29:3-14
  • Valeva A, Hellmann N, Walev I, Strand D, Plate M, Brack A, Hanada K, Decker H, Bhakdi S (2006): "Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore", J. Biol. Chem, 281: 26014 - 26021
  • Decker H, Schweikardt T, Tuczek F (2006): "The first crystal structure of tyrosinase: all questions answered?" Highlight in Angewandte Chemie Engl Ed. 45, 4546 - 4550
  • Hagner-Holler S, Schoen A, Erker W, Marden JH, Rupprecht R, Decker H, Burmester T (2004): "A hemocyanin from an insect", Proc. Natl. Acad. Sci. USA 101:871-874
  • Jaenicke E, Decker H (2004): "Functional changes in the family of type 3 copper proteins in evolution", ChemBioChem. 5:163-176
  • Hartmann H, Bongers A, Decker H (2004): "Monte Carlo based reconstruction of keyhole limpet hemocyanin type 1 (KLH1): Small angle X-ray scattering reveals oxygen dependent conformational change of the surface", J. Biol. Chem. 279:2841-2845
  • Decker H, Jaenicke E (2004): "Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins", Dev. Comp. Immunol. 28:673-87, invited review
  • Lippitz M, Erker W, Decker H, van Holde K, Basche T (2002): "Two-photon spectroscopy and microscopy of tryptophan containing single proteins", Proc. Natl. Acad. Science USA 99:2772-7
  • van Holde K, Miller KI, Decker H (2001): "Hemocyanin and invertebrate evolution", J. Biol. Chem. 276: 15563-15566
  • Decker H, Ryan M, Jaenicke E, Terwilliger N (2001): "SDS induced pheoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum and Cancer magister", J. Biol. Chem. 276: 17796-17799
  • Decker H, Tuczek F (2000): "Phenoloxidase activity of hemocyanins: Activation, substrate orientation and molecular mechanism", Trends in Biochem. Sci. 25:392-397
  • Decker H, Terwilliger N (2000): "COPs and robbers: evolution of copper oxygen proteins", J. Exp. Biol.203:1777-1782
  • Decker H, Dillinger R, Tuczek F (2000): "How does tyrosinase work? Recent insights from model chemistry and structural biology", Angew. Chemie Int. Ed. 39:1587-1591
  • Decker H, Rimke T (1998): "Two different functions of one active site: Binding oxygen and phenoloxidase activity of hemocyanin of tarantula hemocyanin", J.Biol. Chem. 273:25889-25892
  • Sterner R, Decker H (1994): "Inversion of the Bohr effect during oxygen binding to a giant tarantula hemocyanin", Proc. Natl. Acad. Sci. USA 91:4835-4839

    Books:
  • Weuffen W. und Decker H. (Herausgeber) (2004) Thiocyanat – ein bioaktives Ion mit orthomolekularem Charakter, I. S. M. H. Verlag, Sarow 2004; 373 Seiten; ISBN 3-934043-06-2
  • Decker H. and van Holde K. (2011) Oxygen and the Evolution of Life. Springer Verlag, Heidelberg, Berlin 1st Edition., 2011, XI, 172 p., Hardcover, ISBN: 978-3-642-13178-3
  • König H. and Decker H. (2012) Kulturgut Rebe und Wein. Spektrum Akademischer Verlag, Heidelberg, 1st Edition, 242 p.. 200 Abb. in Farbe. Hardcover, ISBN: 978-3-8274-2886-8