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Genomes and Genes | H DeckerSummaryAffiliation: University of Mainz Country: Germany Publications
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Publications
Tarantula hemocyanin shows phenoloxidase activityH 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...
Recent findings on phenoloxidase activity and antimicrobial activity of hemocyaninsHeinz Decker
, , 55099 Mainz, Germany
Dev Comp Immunol 28:673-87. 2004
SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magisterH 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...
Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylusH 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...
Cops and robbers: putative evolution of copper oxygen-binding proteinsH 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)...
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...
Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectorsDorothea 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...
Small-angle scattering techniques for analyzing conformational transitions in hemocyaninsHermann Hartmann
Institute for Molecular Biophysics, Johannes Gutenberg University, Mainz, Germany
Methods Enzymol 379:81-106. 2004
Linked analysis of large cooperative, allosteric systems: the case of the giant HBL hemoglobinsNadja 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...
A respiratory hemocyanin from an insectSilke 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...
Transmission photoemission electron microscopy for lateral mapping of the X-ray absorption structure of a metalloprotein in a liquid cellD 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...
Cockroach allergens Per a 3 are oligomersBeatrice 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...
Tyrosinases from crustaceans form hexamersElmar Jaenicke
, , 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...
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...
Allergological implication of the quaternary hexameric structure of the cockroach allergen Per a 3I 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...
Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: an ITC studyN 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...
Kinetic properties of hexameric tyrosinase from the crustacean Palinurus elephasAntje 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...
Fluorescence labels as sensors for oxygen binding of arthropod hemocyaninsWolfgang 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...
Cooperative transition in the conformation of 24-mer tarantula hemocyanin upon oxygen bindingWolfgang 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...
Immobilization and AFM of single 4 x 6-mer tarantula hemocyanin moleculesWolfgang 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...
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
Similar enzyme activation and catalysis in hemocyanins and tyrosinasesHeinz 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...
A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutationsThorsten 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...
Cupredoxin-like domains in haemocyaninsElmar 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...
Structural characterization of the alpha-hemolysin monomer from Staphylococcus aureusChristian 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...
Tryptophan quenching as linear sensor for oxygen binding of arthropod hemocyaninsWolfgang 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...
Kinetic properties of catecholoxidase activity of tarantula hemocyaninElmar 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...
Bacterial tyrosinasesHarald 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...
Toward oxygen binding curves of single respiratory proteinsWolfgang 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...
Structure-based calculation of multi-donor multi-acceptor fluorescence resonance energy transfer in the 4x6-mer tarantula hemocyaninWolfgang 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...
Conversion of crustacean hemocyanin to catecholoxidaseElmar 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...
Small-angle X-ray scattering-based three-dimensional reconstruction of the immunogen KLH1 reveals different oxygen-dependent conformationsHermann 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...
Nested allosteric interactions in extracellular hemoglobin of the leech Macrobdella decoraNadja 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...
Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californicaElmar 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...
Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in bindingNadja 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...
All hierarchical levels are involved in conformational transitions of the 4 x 6-meric tarantula hemocyanin upon oxygenationHermann 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...
Urate as effector for crustacean hemocyaninsNadja Hellmann
Institute for Molecular Biophysics, University of Mainz, D-55099 Mainz, Germany
Micron 35:109-10. 2004
Modeling techniques for analysing conformational transitions in hemocyanins by small-angle scattering of X-rays and neutronsHermann Hartmann
Institute for Molecular Biophysics, University of Mainz, Jakob Welder Weg 26, D-55128 Mainz, Germany
Micron 35:11-3. 2004
A potential role for water in the modulation of oxygen-binding by tarantula hemocyaninN 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...
Functional changes in the family of type 3 copper proteins during evolutionElmar Jaenicke
, , Jakob Welder Weg 26, 55128 Mainz, Germany
Chembiochem 5:163-9. 2004
Tarantula hemocyanins imaged by atomic force microscopyMarco 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...
A novel mutation in FGFR-3 disrupts a putative N-glycosylation site and results in hypochondroplasiaA 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...
Homology modelling of hemocyanins and tyrosinases: pitfalls in automated approachesThorsten Schweikardt
, , Mainz 55099, Germany
Micron 35:97-8. 2004
Two-photon excitation microscopy of tryptophan-containing proteinsM 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....
Monte Carlo-based rigid body modelling of large protein complexes against small angle scattering dataChristian 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...
Allosteric models for multimeric proteins: oxygen-linked effector binding in hemocyaninMichael 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...
Evidence that clustered phosphocholine head groups serve as sites for binding and assembly of an oligomeric protein poreAngela 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...
Quaternary structure and functional properties of Penaeus monodon hemocyaninMariano 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...
Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurementsGunnar Jeschke
, 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...
Potential active-site residues in polyneuridine aldehyde esterase, a central enzyme of indole alkaloid biosynthesis, by modelling and site-directed mutagenesisEmine Mattern-Dogru
, , , Germany
Eur J Biochem 269:2889-96. 2002..The results showed that PNAE is a novel member of the alpha/beta hydrolase enzyme superfamily...
Molecular mass of macromolecules and subunits and the quaternary structure of hemoglobin from the microcrustacean Daphnia magnaTobias 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...
Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational statesLuca Ronda
Department of Biochemistry and Molecular Biology, University of Parma, Parma, Italy
Gene 398:202-7. 2007..californicum hemocyanin in solution...
Hemocyanin conformational changes associated with SDS-induced phenol oxidase activationSharon Baird
School of Biological and Environmental Sciences, University of Stirling, Stirling FK9 4LA, Scotland, UK
Biochim Biophys Acta 1774:1380-94. 2007....
The Root effect--a physiological perspectiveBernd Pelster
Department of Zoology and Limnology, University of Innsbruck, A-6020 Innsbruck, Austria
Micron 35:73-4. 2004
