Fluorescence labels as sensors for oxygen binding of arthropod hemocyanins

Biochemical and Biophysical Research Communications

Volumn 324, Issue 2, 2004, Pages 893-900

  Erker, Wolfgang ^a   Schoen, Axel ^a   Basché, Thomas ^a   Decker, Heinz ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

5 IAF; Cooperativity; Crayfish; Energy transfer; Fluorescence quenching; FRET; Single molecule spectroscopy; Spiny lobster; TAMRA; Tarantula

Indexed keywords

FLUORESCENT DYE; HEMOCYANIN; OXYGEN;

ARTHROPOD; ARTICLE; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; NONHUMAN; OXYGEN AFFINITY; PHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DETERMINATION; ULTRAVIOLET RADIATION;

ANIMALS; ARTHROPODS; ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENT DYES; HEMOCYANIN; OXYGEN; PALINURIDAE; SPECTROMETRY, FLUORESCENCE; SPIDERS;

ARTHROPODA; ASTACOIDEA; LOBSTER; PONTOPHILUS SPINOSUS;

EID: 5144221789     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.138     Document Type: Article

References (30)

1. K.E. van Holde, and K.I. Miller Hemocyanins Adv. Protein Chem. 47 1995 1 81
2. K.E. van Holde, K.I. Miller, and H. Decker Hemocyanins and invertebrate evolution J. Biol. Chem. 276 2001 15563 15566
3. W.P.J. Gaykema, W.G.J. Hol, J.M. Vereijken, N.M. Soeter, H.J. Bak, and J.J. Beintema 3.2 A structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin Nature 309 1984 23 29
4. B. Hazes, K.A. Magnus, C. Bonaventura, J. Bonaventura, Z. Dauter, K.H. Kalk, and W.G. Hol Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation Protein Sci. 2 1993 597 619
5. A. Volbeda, and W.G. Hol Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution J. Mol. Biol. 209 1989 249 279
6. K.A. Magnus, B. Hazes, H. Ton-That, C. Bonaventura, J. Bonaventura, and W.G. Hol Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences Proteins 19 1994 302 309
7. M.J. Baldwin, D.E. Root, J.E. Pate, K. Fujisawa, N. Kitajima, and E.I. Solomon Spectroscopic studies of a side-on peroxide-bridged binuclear copper(II) model complex of relevance to the active sites in oxyhemocyanin and oxytyrosinase J. Am. Chem. Soc. 114 1992 10421 10431
8. N. Kitajima, K. Fujisawa, C. Fujimoto, Y. Moro-oka, S. Hashimoto, T. Kitagawa, K. Toriumi, K. Tatsumi, and A. Nakamura A new model for dioxygen binding in hemocyanin: synthesis, characterization, and molecular structure of the μ-h2:h2-peroxo dinuclear copper(II) complexes [Cu(HB(3,5-R2pz)3)]2(O2) (R = i-Pr and Ph) J. Am. Chem. Soc. 114 1992 1277 1291
9. M.E. Cuff, K.I. Miller, K.E. van Holde, and W.A. Hendrickson Crystal structure of a functional unit from Octopus hemocyanin J. Mol. Biol. 278 1998 855 870
10. R. Loewe Hemocyanins in spiders V: fluorimetric recording of oxygen binding curves, and its application to the analysis of allosteric interactions in Eurypelma californicum hemocyanin J. Comp. Physiol. 128 1978 161 168
11. R.H. Holm, P. Kennepohl, and E.I. Solomon Structural and functional aspects of metal sites in biology Chem. Rev. 96 1996 2239 2314
12. B. Richey, H. Decker, and S.J. Gill A direct test of the linearity between optical density change and oxygen binding in hemocyanins E.J. Wood Life Chemistry Reports, Supplement 1 1983 Harwood Academic Chur, London, New York 309 312
13. N. Shaklai, and E. Daniel Fluorescence properties of hemocyanin from Levantina hierosolima Biochemistry 9 1970 564 568
14. W. Erker, R. Hübler, and H. Decker Structure-based calculation of multi-donor multi-acceptor fluorescence resonance energy transfer in the 4 x 6-mer tarantula hemocyanin Eur. Biophys. J. 33 2004 386 395
15. W. Erker, R. Hübler, H. Decker, Tryptophan quenching by FRET as linear sensor for oxygen binding of hemocyanins, submitted
16. W. Erker, M. Lippitz, T. Basché, and H. Decker Toward oxygen binding curves of single respiratory proteins Micron 35 2004 111 113
17. A. Mazzini, M. Beltramini, R. Favilla, P. Cavatorta, P. Dimuro, and B. Salvato An oxygenation-sensitive dye binding to Carcinus maenas hemocyanin Biophys. Chem. 52 1994 145 156
18. J. Markl, B. Kempter, B. Linzen, M.M. Bijlholt, and E.F. van Bruggen Hemocyanins in spiders, XVI[1]. Subunit topography and a model of the quaternary structure of Eurypelma hemocyanin Hoppe Seylers Z. Physiol. Chem. 362 1981 1631 1641
19. R. Voit, G. Feldmaier-Fuchs, T. Schweikardt, H. Decker, and T. Burmester Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits J. Biol. Chem. 275 2000 39339 39344
20. H. Decker, and R. Föll Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus Comp. Biochem. Physiol. A Mol. Integr. Physiol. 127 2000 147 154
21. J. Markl Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods Biol. Bull. 171 1986
22. W. Stöcker, R. Raeder, M.M. Bijolt, T. Wichertjes, E.F.J. van Bruggen, and J. Markl The quaternary structure of four crustacean two-hexameric hemocyanins: Immunocorrelation, stoichiometry, reassembly and topology of individual subunits J. Comp. Physiol. B 158 1988 271 289
23. U. Meissner, M. Stohr, K. Kusche, T. Burmester, H. Stark, J.R. Harris, E.V. Orlova, and J. Markl Quaternary structure of the European spiny lobster (Palinurus elephas) 1 x 6-mer hemocyanin from cryoEM and amino acid sequence data J. Mol. Biol. 325 2003 99 109
24. B.W. van der Meer, G. Coker, and S.Y.S. Chen Resonance Energy Transfer 1994 VCH New York
25. R. Boteva, F. Ricchelli, G. Sartor, and H. Decker Fluorescence properties of hemocyanin from tarantula (Eurypelma californicum): a comparison between the whole molecule and isolated subunits J. Photochem. Photobiol. B Biol. 17 1993 145 153
26. R.Y. Tsien, A. Waggoner, Fluorophors for confocal microscopy: photophysics and photochemistry, in: J.B. Pawley, (Ed.), Handbook of Biological Confocal Microscopy, Plenum Press, New York, 1990, p. 169
27. R.P. Haugland Handbook of Fluorescenct Probes and Research Products ninth ed. 2002 Molecular Probes Eugene
28. M. Lippitz, W. Erker, H. Decker, K.E. van Holde, and T. Basché Two-photon excitation microscopy of tryptophan-containing proteins Proc. Natl. Acad. Sci. USA 99 2002 2772 2777
29. H. Decker, and F. Tuczek Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism Trends Biochem. Sci. 25 2000 392 397
30. A. Sanchez-Ferrer, J.N. Rodriguez-Lopez, F. Garcia-Canovas, and F. Garcia-Carmona Tyrosinase: a comprehensive review of its mechanism Biochim. Biophys. Acta 1247 1995 1 11