Mitglied des FZI   Univ.-Prof. (C4) Dr. rer. nat. Heinz Decker Institut für Molekulare Biophysik Johannes-Gutenberg-Universität Mainz Jakob Welder Weg.26, 55128 Mainz, Germany Email: hdecker@uni-mainz.de Phone: 0049-6131-3923570/1 (Sekr.) Studium und akademischer Werdegang:

1971–1976 Studium der Biologie und Physik an der Ludwig Maximilians Universität München (LMU)

1981 Dr. rer. nat: (LMU) 1982-1983 Wiss. Mitarbeiter, Dept. of Chem. & Biochem., Univ.of Colorado,

Boulder, CO, U.S.A. 1983-1984 Res. Assistant Professor, School of Medicine, St. Louis University,

MO, U.S.A. 1984-1985 Wiss. Mitarbeiter, MPI für Medizinische Wissenschaft, Abt. für

Biophysik, Heidelberg 1985-1994 Projektleiter für Molekulare Physiologie and Biophysik, seit 1991 C2

a.Z. am Institut für Biologie, LMU 1993 Ruf auf C3-Professur (Listenplatz 1), Universität Hannover,

abgelehnt 1993–1994 C4-Professor (komm.) (Institut für Zoologie, Tiermedizinische

Hochschule Hannover TiHo) 1994 Gastprofessor, Institute of Biology, University of Padova, Italy since 1995 C4-Professor für Molekulare Biophysik und Institutsleitung, JGU

Mainz 1998 Sabbatical: Oregon Institute of Marine Biology, University of Oregon,

University of Padua, Italy 2006 Sabbatical: Marine Biology Laboratory Woods Hole, MA, USA

Forschungsinteressen: Biophysics and biochemistry of multisubunit metallo proteins (hemocyanins, tyrosinase, extracellular hemoglobins) and their importance for immunology and allergology; pore building process in natural and artificial membranes by alpha toxin; cooperativity and allostery phenomena; structural biology (3D reconstruction of proteins, homology modelling, X-ray crystallography, electron microscopy, small angle scattering with x-rays (SAXS) and neutrons (SANS), bioinformatics, molecular dynamics); nanobiotechnological applications of proteins; biofunctionalizing surfaces.

Mitglied des FZI Mitgliedschaften (Auswahl seit 2002):

• SFB 490 Invasion & Persistence at Infections: D4 (Hellmann, Decker): Pore building mechanism (2006-11)

• SFB 625 From single molecules to nanoscopic structured materials: B2 (Decker, Markl, Schönehense) Surface bound hemocyanins (2002-2005)

• DFG Graduate School 1043: Antigenspezifische Immuntherapie: B2 (Decker) Crystal structure and SAXS of hemocyanin. (2004-14)

• BMBF Center Multifunctional materials and miniaturised devices: (2001-03); Coordinator of TG 4: Biosensoren, Projekt 4-1 (Decker): Nanosensor Hämocyanin

• BMBF 05 KS1UMA/4 (Decker): Dynamics of hemocyanins with small angle scattering (2001-04)

• BMBF 05 KS7UMA (Langguth, Nawroth, Decker, Frey) Indirect radiation therapy of cancer with target-nanoparticles (2007-2013

• BMWi/FEI (Dietrich, Will, Wigand, Decker): Special proteins in wine and juice (2011-14)

• Stiftung Innovation Rheinland-Pfalz 929 I+II Intolerance to wine (2010-12 • Stiftung Innovation Rheinland-Pfalz 1051 (Decker, König) Action of oxidizing

enzymes on colour, sensoric and other healthy ingredients of wine (2013-14) • EU COST D21: Molecular oxygen activation at biological and biomimetic metal

centres (2001-06) • EU COST Action: CM1003 WG2: Biological oxidation reactions utilizing

dioxygen as oxidants (2011-14)

Bücher Weuffen W. and Decker H. (editors) (2004) Thiocyanat – ein bioaktives Ion mit

orthomolekularem Charakter, I. S. M. H. Verlag, Sarow 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

Publikationen (Auswahl): Fronk P., Blettner M., Decker H. (2013) Self-reported consumption of wine and other

alcoholic beverages in a German wine area, Intl 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

Mitglied des FZI 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

Wigand P, Blettner M, Saloga J, Decker H (2012) Prevalence of wine intolerance:

results of a survey from Mainz, Germany. Dtsch Arztebl Int 109:437-444 Jaenicke E, Pairet B, Hartmann H, Decker H. (2012) Crystallization and preliminary

analysis of crystals of the 24-meric hemocyanin of the emperor scorpion (Pandinus imperator). PLoS One. 2012;7(3):e32548. Epub 2012 Mar 5

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

Wigand P., Blettner M., Decker H (2012) Rot-, Rose- und Weinweinkonsum in einer

deutschen Weinregion. Deutsche Lebensmittel-Rundschau 108:467-470 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

Mindykovski B., Jaenicke E.,, Tenzer S., Cirak S., Schweikardt T., Schild H.-J., Decker

H. (2010) Cockroach allergens Per a 3 are oligomers, Dev. Comp. Immunol. 34:722-733

Panzer D., Beck C., Greil S., Hahn M., Maul J., Schönhense G., Decker H., Aziz E.F.

(2010) Water influences the copper active site in hemocyanin, The Journal of Physical Chemistry Letters 1: 1642–1647

Wigand P., Tenzer S., Schild HJ., Decker H. (2009) Analysis of protein composition

of red wine in comparison with rose and white wines by electrophoresis and high-pressure liquid chromatography-mass spectrometry (HPLC-MS). Journal of Agricultural and Food Chemistry, 57(10): 4328-4333

Jaenicke E, Fraune S, May S. Irmak P., Augustin R. Meesters C., Decker H. Zimmer

M. (2009) Is activated hemocyanin instead of phenoloxidase involved in immune response in woodlice? Dev Comp Imm. 33: 1055–1063

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 J M, Decker H, Hartmann H, Chavan B, Rokos H., Spencer JD, Hasse S,

Thornton J, Shalbaf M, Paus R and Schallreuter K U (2009) Senile hair greying: H2O2-mediated oxidative stress affects human hair colour by blunting methionine sulfoxide repair. FASEB J. 23: 2065-2075

Mitglied des FZI Cong Y., Ludtke S.J., Woolford D. S. A., Khant H. A., 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

Nillius D, Jaenicke E, Decker H, (2008) Switch between tyrosinase and

catecholoxidase activity of scorpion hemocyanin, FEBS Letters 582: 749–754 Bellinghausen J., Häringer B, Lafargue B, Strand D, König B, Knop J, Decker H and

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

Decker H., Schweikardt T., Nillius D., Salzbrunn U., Jaenicke E. and 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. and Markl. J. (2007)

Minireview: Recent insights in the structure, function and evolution of hemocyanins. Integrative and Comparative Biology, 47: 631-644

Claus H. and Decker H. (2006): Bacterial Tyrosinases. Systematic and Applied

Microbiology, 29:3-14 Decker H., Schweikardt T. and Tuczek F (2006) The first crystal structure of

tyrosinase: all questions answered? Highlight in Angewandte Chemie Engl Ed., 45, 4546 – 4550

Valeva A., Hellmann N., Walev I., Strand D., Plate M., Boukhallouk, Brack A.,F.,

Hanada K., Decker H., and 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

Jeschke G., Bender A., Schweikardt T., Panek G., Decker H. and Paulsen (2005)

Localisation of the N-terminal domain in light-harvesting chlorophyll a/b protein (LHCIIb) by electron paramagnetic resonance (EPR) measurements, J. Biol. Chem., 280, 18623-30

Jaenicke E. and H. Decker (2004): Functional changes in the family of type 3 copper

proteins in evolution. ChemBioChem. 5:163-176 Decker H. and E. Jaenicke (2004): Recent findings on phenoloxidase activity and

antimicrobial activity of hemocyanins. Dev. Comp. Immunol. 28:673-87 Hartmann H., A. Bongers, H. Decker (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

Mitglied des FZI Hartmann H. and Decker H (2004): Small-angle scattering techniques for analysing

structural transitions in hemocyanins. Methods in Enzymology Vol 379 “Energetics of Biological Macromolecules”, eds. J. M. Holt, M. L. Johnson, G. K. Ackers, pp. 81-106

Hagner-Holler S., A. Schoen, W. Erker, J.H. Marden, R. Rupprecht, H. Decker, T.

Burmester (2004) A hemocyanin from an insect Proc. Natl. Acad. Sci. USA 101, 871-874

Brack A., Strube J., Stolz P. And Decker H. (2003): Effects of ultra high dilutions of

3,5-dichlorophenol on the luminescence of the bacteria Vibrio fischeri, Biochi. Biophys. Acta 1621:253– 260

Mattern-Dogru E., Ma X., Hartmann H., Decker H. and Stöckigt J. (2002): Potential

active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesis. Eur. J. Biochem 269:2889-2896.

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. Sci. USA 99, 2772-7

Decker H., M. Ryan, E. Jaenicke and N. Terwilliger (2001): SDS induced

pheoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum and Cancer magister. J. Biol. Chem. 276: 17796-17799

van Holde K, K. I. Miller and H. Decker (2001): Hemocyanin and invertebrate

evolution. J. Biol. Chem. 276: 15563-15566 Decker H. and N. Terwilliger (2000): COPs and robbers: evolution of copper oxygen

proteins. J. Exp. Biol.203:1777-1782 Decker H., R. Dillinger, Tuczek F. (2000) How does tyrosinase work? Recent insights

from model chemistry and structural biology Angewandte Chemie Int. Ed. 39,1587-1591

Decker H., Tuczek F. (2000) Phenoloxidase activity of hemocyanins: Activation,

substrate orientation and molecular mechanism. Trends in Biochem. Sci. 25:392-397

Decker H. and T. Rimke (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. and H. Decker (1994). Inversion of the Bohr effect during oxygen binding

to a giant tarantula hemocyanin. Proc. Natl. Acad. Sci. USA 91:4835-4839 Markl J. and H. Decker (1992). Molecular structure of arthropodan hemocyanins.

Advances in Comparative and Environmental Physiology 13:325-376

Mitglied des FZI Decker H. and R. Sterner (1990). Nested allostery of Arthropodan hemocyanin

(Eurypelma californicum and Homarus americanus): The role of the protons. J. Mol. Biol. 211:281-293

Robert C.H., H. Decker, B. Richey, S.J. Gill and J. Wyman (1987). Nesting:

Hierarchies of allosteric interactions. Proc. Natl. Acad. Sci. (USA) 84:1891-1895