H Decker

Summary

Affiliation: University of Mainz
Country: Germany

Publications

  1. ncbi request reprint Tarantula hemocyanin shows phenoloxidase activity
    H Decker
    Institute for Molecular Biophysics, University of Mainz, Welder Weg 26, D 55128 Mainz, Germany
    J Biol Chem 273:25889-92. 1998
  2. ncbi request reprint Cops and robbers: putative evolution of copper oxygen-binding proteins
    H Decker
    Institute for Molecular Biophysics, University of Mainz, Germany
    J Exp Biol 203:1777-82. 2000
  3. ncbi request reprint Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins
    Heinz Decker
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Dev Comp Immunol 28:673-87. 2004
  4. ncbi request reprint Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus
    H Decker
    Institute for Molecular Biophysics, University of MainzJacob Welder Weg 26, D 55099, Mainz, Germany
    Comp Biochem Physiol A Mol Integr Physiol 127:147-54. 2000
  5. ncbi request reprint SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister
    H Decker
    Institute for Molecular Biophysics, University of Mainz, D55128 Mainz, Germany
    J Biol Chem 276:17796-9. 2001
  6. doi request reprint Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors
    Dorothea Nillius
    Institut für Molekulare Biophysik der Johannes Gutenberg Universität Mainz, Jakob Welder Weg 26, Mainz, Germany
    FEBS Lett 582:749-54. 2008
  7. doi request reprint Is activated hemocyanin instead of phenoloxidase involved in immune response in woodlice?
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Dev Comp Immunol 33:1055-63. 2009
  8. ncbi request reprint Small-angle scattering techniques for analyzing conformational transitions in hemocyanins
    Hermann Hartmann
    Institute for Molecular Biophysics, Johannes Gutenberg University, Mainz, Germany
    Methods Enzymol 379:81-106. 2004
  9. doi request reprint Linked analysis of large cooperative, allosteric systems: the case of the giant HBL hemoglobins
    Nadja Hellmann
    Institute for Molecular Biophysics, Johannes Gutenberg University, Mainz, Germany
    Methods Enzymol 436:463-85. 2008
  10. pmc A respiratory hemocyanin from an insect
    Silke Hagner-Holler
    Institutes of Zoology and Molecular Biophysics, Johannes Gutenberg University of Mainz, 55099 Mainz, Germany
    Proc Natl Acad Sci U S A 101:871-4. 2004

Collaborators

Detail Information

Publications55

  1. ncbi request reprint Tarantula hemocyanin shows phenoloxidase activity
    H Decker
    Institute for Molecular Biophysics, University of Mainz, Welder Weg 26, D 55128 Mainz, Germany
    J Biol Chem 273:25889-92. 1998
    ..Therefore no new arrangement of the active site, with its two copper atoms and the mu - eta2:eta2 bound O2 molecule, is necessary to develop the catalytic function...
  2. ncbi request reprint Cops and robbers: putative evolution of copper oxygen-binding proteins
    H Decker
    Institute for Molecular Biophysics, University of Mainz, Germany
    J Exp Biol 203:1777-82. 2000
    ..Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs)...
  3. ncbi request reprint Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins
    Heinz Decker
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Dev Comp Immunol 28:673-87. 2004
  4. ncbi request reprint Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus
    H Decker
    Institute for Molecular Biophysics, University of MainzJacob Welder Weg 26, D 55099, Mainz, Germany
    Comp Biochem Physiol A Mol Integr Physiol 127:147-54. 2000
    ..The oxygen binding behaviour of di-hexameric hemocyanins from cold and warm adapted animals do not show differences with respect to affinity, Bohr effect and cooperativity...
  5. ncbi request reprint SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister
    H Decker
    Institute for Molecular Biophysics, University of Mainz, D55128 Mainz, Germany
    J Biol Chem 276:17796-9. 2001
    ..The chelicerate hemocyanin subunits showing phenoloxidase activity may have evolved into a separate phenoloxidase in crustaceans...
  6. doi request reprint Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors
    Dorothea Nillius
    Institut für Molekulare Biophysik der Johannes Gutenberg Universität Mainz, Jakob Welder Weg 26, Mainz, Germany
    FEBS Lett 582:749-54. 2008
    ..This demonstrates that substrate specificity is not caused by a chemical modification of the active site...
  7. doi request reprint Is activated hemocyanin instead of phenoloxidase involved in immune response in woodlice?
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Dev Comp Immunol 33:1055-63. 2009
    ..We propose a peracarid-type hemocyanin that may have evolved in response to its required multiple functions in respiration and immune response, while phenoloxidase sensu strictu is lacking...
  8. ncbi request reprint Small-angle scattering techniques for analyzing conformational transitions in hemocyanins
    Hermann Hartmann
    Institute for Molecular Biophysics, Johannes Gutenberg University, Mainz, Germany
    Methods Enzymol 379:81-106. 2004
  9. doi request reprint Linked analysis of large cooperative, allosteric systems: the case of the giant HBL hemoglobins
    Nadja Hellmann
    Institute for Molecular Biophysics, Johannes Gutenberg University, Mainz, Germany
    Methods Enzymol 436:463-85. 2008
    ..Possible advantages of a hierarchical cooperative model compared to a linear extension of the MWC model are discussed...
  10. pmc A respiratory hemocyanin from an insect
    Silke Hagner-Holler
    Institutes of Zoology and Molecular Biophysics, Johannes Gutenberg University of Mainz, 55099 Mainz, Germany
    Proc Natl Acad Sci U S A 101:871-4. 2004
    ..However, our results demonstrate that, in contrast to the accepted paradigm, certain basal insects have retained an ancestral blood-based mechanism of gas exchange...
  11. ncbi request reprint Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
    H Decker
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat Mainz, D 55099 Mainz, Germany
    Trends Biochem Sci 25:392-7. 2000
    ..On the basis of their molecular structures, hemocyanins are used as model systems to understand the substrate-active-site interaction between catecholoxidases and tyrosinases...
  12. doi request reprint Cockroach allergens Per a 3 are oligomers
    Beatrice Mindykowski
    Institute for Molecular Biophysics, University of Mainz, Jakob Welder Weg 26, Mainz, Germany
    Dev Comp Immunol 34:722-33. 2010
    ..We propose this might contribute to their allergic potential as well as their extreme stability with respect to temperature...
  13. pmc Tyrosinases from crustaceans form hexamers
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat Mainz, Jakob Welder Weg 26, D 55128 Mainz, Germany
    Biochem J 371:515-23. 2003
    ..The hexameric nature of arthropod tyrosinases suggests that these proteins were the ideal predecessors from which to develop the oxygen-carrier protein haemocyanin, with its allosteric and co-operative properties, later on...
  14. doi request reprint Transmission photoemission electron microscopy for lateral mapping of the X-ray absorption structure of a metalloprotein in a liquid cell
    D Panzer
    Institut fur Physik, Johannes Gutenberg Universitat, Staudinger Weg 7, Mainz, Germany
    Eur Biophys J 38:53-8. 2008
    ..In this way, different copper valencies are laterally distinguished under in vivo-like conditions, attributed to Cu(I) in the deoxy-state and Cu(II) in the oxy-state...
  15. ncbi request reprint Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1)
    H Hartmann
    , , Germany
    Eur Biophys J 30:471-5. 2001
    ..Upon oxygenation, KLH1 becomes smaller and more compact. Model reconstruction of KLH1 indicates a hollow cylinder with two rings located close to both ends, which move slightly together upon oxygenation...
  16. ncbi request reprint Allergological implication of the quaternary hexameric structure of the cockroach allergen Per a 3
    I Bellinghausen
    Department of Dermatology, University of Mainz, Mainz, Germany
    Clin Exp Allergy 38:539-48. 2008
    ..Cockroach allergens play a very important role in allergic diseases, especially asthma. The major allergen of the American cockroach (Periplaneta americana), Per a 3, naturally occurs as isoforms of hexamers...
  17. ncbi request reprint Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: an ITC study
    N Hellmann
    Institute of Molecular Biophysics, J Mainz, Germany
    Biophys Chem 90:279-99. 2001
    ..leptodactylus. The two binding sites differ strongly in their specificity towards the two analogues. It can be hypothesized that two different subunit types (beta and gamma) are responsible for the two types of binding sites...
  18. ncbi request reprint Fluorescence labels as sensors for oxygen binding of arthropod hemocyanins
    Wolfgang Erker
    Institute for Physical Chemistry, Johannes Gutenberg University, Mainz, Germany
    Biochem Biophys Res Commun 324:893-900. 2004
    ..In addition, another novel application is provided by these labels, i.e., the investigation of the influence of effectors by recording simultaneously the binding of oxygen in the visible and of effectors in the UV...
  19. doi request reprint Kinetic properties of catecholoxidase activity of tarantula hemocyanin
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Mainz, Germany
    FEBS J 275:1518-28. 2008
    ..This indicates that the activated hemocyanin behaves as a normal phenoloxidase...
  20. ncbi request reprint Cooperative transition in the conformation of 24-mer tarantula hemocyanin upon oxygen binding
    Wolfgang Erker
    Department of Physical Chemistry, Johannes Gutenberg University, Mainz, Welderweg 11, 55099 Mainz, Germany
    J Biol Chem 280:12391-6. 2005
    ..Based on the agreement between oxygen binding curves and fluorescence titration we concluded that Prodan monitors a conformational transition of the allosteric unit...
  21. ncbi request reprint Bacterial tyrosinases
    Harald Claus
    Institute for Microbiology and Wine Research, University of Mainz, Becherweg 15, D 55099 Mainz, Germany
    Syst Appl Microbiol 29:3-14. 2006
    ..This review summarizes the present knowledge of bacterial tyrosinases, which are promising models in order to get more insights in structure, enzymatic reactions and functions of "type 3 copper" proteins in general...
  22. ncbi request reprint Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin molecules
    Wolfgang Erker
    Institute for Physical Chemistry, University Mainz, Germany
    Micron 37:735-41. 2006
    ..This study is a step in resolving conformational heterogeneities, involved in oxygen binding of hemocyanins, at the single-molecule level by AFM...
  23. ncbi request reprint The first crystal structure of tyrosinase: all questions answered?
    Heinz Decker
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Angew Chem Int Ed Engl 45:4546-50. 2006
  24. ncbi request reprint A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations
    Thorsten Schweikardt
    Institute of Molecular Biophysics, University of Mainz, Mainz, Germany
    Pigment Cell Res 20:394-401. 2007
    ..Therefore, our model explains the mechanistic necessity for conservation of not only active site histidines but also adjacent amino acids in tyrosinase...
  25. ncbi request reprint Toward oxygen binding curves of single respiratory proteins
    Wolfgang Erker
    Institute for Physical Chemistry, University of Mainz, Welderweg 11, Mainz 55128, Germany
    Micron 35:111-3. 2004
    ..The dye's fluorescence is quenched due to Förster energy transfer to the oxygenated active sites of hemocyanin...
  26. ncbi request reprint Urate as effector for crustacean hemocyanins
    Nadja Hellmann
    Institute for Molecular Biophysics, University of Mainz, D 55099 Mainz, Germany
    Micron 35:109-10. 2004
  27. doi request reprint Kinetic properties of hexameric tyrosinase from the crustacean Palinurus elephas
    Antje Brack
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Mainz, Germany
    Photochem Photobiol 84:692-9. 2008
    ..These observations lead to the hypothesis that a secondary, allosteric binding site exists, which binds dopamine and PTU and reduces the catalytic activity...
  28. doi request reprint Cupredoxin-like domains in haemocyanins
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Jakob Welder Weg 26, 55128 Mainz, Germany
    Biochem J 426:373-8. 2010
    ..We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain...
  29. ncbi request reprint All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenation
    Hermann Hartmann
    Institut für Molekulare Biophysik, Universitat Mainz, Jakob Welder Weg 26, D 55099 Mainz, Germany
    Biochim Biophys Acta 1601:132-7. 2002
    ..It also shows a concept of allosteric interaction in hierarchically assembled proteins to guarantee the involvement of all subunits of a native oligomer to establish very high Hill coefficients...
  30. ncbi request reprint Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in binding
    Nadja Hellmann
    Institute for Molecular Biophysics, University of Mainz, Germany
    Biochim Biophys Acta 1599:45-55. 2002
    ..Furthermore, the model also includes the existence of a conformation with very high ATPase activity. Such a conformation might be of importance at a certain stage in the folding cycle...
  31. pmc Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californica
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Biochem J 375:681-8. 2003
    ..Thus both proteins might belong to a new class of haemolymph proteins present in the haemolymph of marine gastropods...
  32. ncbi request reprint Nested allosteric interactions in extracellular hemoglobin of the leech Macrobdella decora
    Nadja Hellmann
    Institute for Molecular Biophysics, University of Mainz, Jakob Welder Weg 26, 55128 Mainz, Germany
    J Biol Chem 278:44355-60. 2003
    ..Thus, besides hemocyanins and GroEL, the hexagonal bilayer hemoglobins represent another class of proteins in which the hierarchical quaternary structure provides the basis for nested interaction in their functional properties...
  33. ncbi request reprint Small-angle X-ray scattering-based three-dimensional reconstruction of the immunogen KLH1 reveals different oxygen-dependent conformations
    Hermann Hartmann
    Institut für Molekulare Biophysik, Universitat Mainz, D 55099 Mainz, Germany
    J Biol Chem 279:2841-5. 2004
    ..Upon oxygenation, the KLH1 molecule becomes longer and skinnier. This study provides the first real evidence how a molluscan hemocyanin changes conformation during an allosteric transition...
  34. ncbi request reprint Structure-based calculation of multi-donor multi-acceptor fluorescence resonance energy transfer in the 4x6-mer tarantula hemocyanin
    Wolfgang Erker
    Institute for Molecular Biophysics, Johannes Gutenberg University, Jakob Welder Weg 26, 55128 Mainz, Germany
    Eur Biophys J 33:386-95. 2004
    ..This results explain for the first time, on a molecular basis, why fluorescence quantum yield can be used as an intrinsic signal for oxygen load of at least one arthropod hemocyanin, in particular that from the tarantula...
  35. doi request reprint Structural characterization of the alpha-hemolysin monomer from Staphylococcus aureus
    Christian Meesters
    Institute of Molecular Biophysics, University of Mainz, Mainz, Germany
    Proteins 75:118-26. 2009
    ..This structure reveals details of the monomeric conformation of the alpha-hemolysin, for example inherent flexibility, along with definite differences in comparison to the structures used as templates...
  36. ncbi request reprint Modeling techniques for analysing conformational transitions in hemocyanins by small-angle scattering of X-rays and neutrons
    Hermann Hartmann
    Institute for Molecular Biophysics, University of Mainz, Jakob Welder Weg 26, D 55128 Mainz, Germany
    Micron 35:11-3. 2004
  37. doi request reprint Tryptophan quenching as linear sensor for oxygen binding of arthropod hemocyanins
    Wolfgang Erker
    Institute of Physical Chemistry, Jakob Welderweg 11, 55099 Mainz, Germany
    Biochim Biophys Acta 1780:1143-7. 2008
    ..It can be used as a model-free signal to investigate oxygen binding of hemocyanins at all aggregation levels. Furthermore it may provide a new way to analyse oxygen binding of phenoloxidases...
  38. ncbi request reprint Conversion of crustacean hemocyanin to catecholoxidase
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Micron 35:89-90. 2004
    ..Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess the ability of catecholoxidase activity...
  39. ncbi request reprint Similar enzyme activation and catalysis in hemocyanins and tyrosinases
    Heinz Decker
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, 55099 Mainz, Germany
    Gene 398:183-91. 2007
    ..Minor conformational differences at the active site seem to decide about whether the active site is only able to oxidize diphenols as in catecholoxidase or if it is also able to o-hydroxylate monophenols as in tyrosinase...
  40. ncbi request reprint A potential role for water in the modulation of oxygen-binding by tarantula hemocyanin
    N Hellmann
    Institute for Molecular Biophysics, University of Mainz, Jakob Welder Weg 26, Mainz 55128, Germany
    Comp Biochem Physiol A Mol Integr Physiol 136:725-34. 2003
    ..The results corroborate the presence of hierarchically organized interactions in this hemocyanin...
  41. ncbi request reprint Functional changes in the family of type 3 copper proteins during evolution
    Elmar Jaenicke
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Jakob Welder Weg 26, 55128 Mainz, Germany
    Chembiochem 5:163-9. 2004
  42. ncbi request reprint Tarantula hemocyanins imaged by atomic force microscopy
    Marco Möller
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Mainz 55099, Germany
    Micron 35:15-6. 2004
    ..Although the resolution was low, the hexamers and topological arrangement within the oligomers can be seen. However, the relative humidity seems to affect the height profiles...
  43. ncbi request reprint A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasia
    A Winterpacht
    Children s Hospital, University of Mainz, D 55101 Mainz, Germany
    Physiol Genomics 2:9-12. 2000
    ..The amino acid exchange itself most probably has no impact on the three-dimensional structure of the receptor domain, suggesting that the phenotype is the result of altered receptor glycosylation and its pathophysiological consequences...
  44. ncbi request reprint Homology modelling of hemocyanins and tyrosinases: pitfalls in automated approaches
    Thorsten Schweikardt
    Institut für Molekulare Biophysik, Johannes Gutenberg Universitat, Mainz 55099, Germany
    Micron 35:97-8. 2004
  45. pmc Two-photon excitation microscopy of tryptophan-containing proteins
    M Lippitz
    Institute of Physical Chemistry, Jakob Welder Weg 11, and Institute of Molecular Biophysics, Jakob Welder Weg 26, University of Mainz, 55099 Mainz, Germany
    Proc Natl Acad Sci U S A 99:2772-7. 2002
    ....
  46. doi request reprint Monte Carlo-based rigid body modelling of large protein complexes against small angle scattering data
    Christian Meesters
    Institute for Molecular Biophysics, Jakob Welder Weg 26, 55126 Mainz, Germany
    Comput Biol Chem 34:158-64. 2010
    ..Features include rigid body modelling to result in static structures and three-dimensional probability densities using two different algorithms...
  47. ncbi request reprint Potential active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesis
    Emine Mattern-Dogru
    Lehrstuhl fur Pharmazeutische Biologie, Institut fur Pharmazie, Johannes Gutenberg Universitat Mainz, Germany
    Eur J Biochem 269:2889-96. 2002
    ..The results showed that PNAE is a novel member of the alpha/beta hydrolase enzyme superfamily...
  48. ncbi request reprint Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states
    Luca Ronda
    Department of Biochemistry and Molecular Biology, University of Parma, Parma, Italy
    Gene 398:202-7. 2007
    ..californicum hemocyanin in solution...
  49. ncbi request reprint Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurements
    Gunnar Jeschke
    Max Planck Institut fur Polymerforschung, Postfach 3148, 55021 Mainz, Germany
    J Biol Chem 280:18623-30. 2005
    ..A similar phosphorylation-induced conformational change of the N-terminal domain has been observed by others in bovine annexin IV which, due to the conformational switch, also loses its membrane-aggregating property...
  50. ncbi request reprint Quaternary structure and functional properties of Penaeus monodon hemocyanin
    Mariano Beltramini
    Department of Biology, University of Padova, Padova, Italy
    FEBS J 272:2060-75. 2005
    ..Under hypoxic conditions, the hexamers are expected not to be completely loaded with oxygen. Here, the dodecamers are supposed to be responsible for the oxygen supply...
  51. ncbi request reprint Allosteric models for multimeric proteins: oxygen-linked effector binding in hemocyanin
    Michael A Menze
    Institut fur Zoophysiologie, Heinrich Heine Universitat, Universitatsstrasse 1, 40225 Dusseldorf, Germany
    Biochemistry 44:10328-38. 2005
    ..vulgaris only during hypoxic conditions, i.e., either during environmental oxygen limitation or extensive exercise...
  52. ncbi request reprint Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein pore
    Angela Valeva
    Institute of Medical Microbiology and Hygiene, Hochhaus am Augustusplatz, D 55101 Mainz, Germany
    J Biol Chem 281:26014-21. 2006
    ..The principle of membrane targeting in the absence of any genuine, high affinity receptor may also underlie the assembly of other lipid-inserted oligomers including cytotoxic peptides, protein toxins, and immune effector molecules...
  53. ncbi request reprint Molecular mass of macromolecules and subunits and the quaternary structure of hemoglobin from the microcrustacean Daphnia magna
    Tobias Lamkemeyer
    Institut fur Zoophysiologie, Westfalische Wilhelms Universitat, Munster, Germany
    FEBS J 273:3393-410. 2006
    ..It turned out to be much more complex than hitherto proposed: it displays D4 symmetry with a diameter of approximately 12 nm and a height of about 8 nm...
  54. ncbi request reprint Hemocyanin conformational changes associated with SDS-induced phenol oxidase activation
    Sharon Baird
    School of Biological and Environmental Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK
    Biochim Biophys Acta 1774:1380-94. 2007
    ....
  55. ncbi request reprint The Root effect--a physiological perspective
    Bernd Pelster
    Department of Zoology and Limnology, University of Innsbruck, A 6020 Innsbruck, Austria
    Micron 35:73-4. 2004