Tryptophan quenching as linear sensor for oxygen binding of arthropod hemocyanins

Biochimica et Biophysica Acta - General Subjects

Volumn 1780, Issue 10, 2008, Pages 1143-1147

  Erker, Wolfgang ^a   Hübler, Rüdiger ^a   Decker, Heinz ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Energy transfer; Fluorescence; FRET; phenoloxidase; Spiny lobster; Tarantula

Indexed keywords

HEMOCYANIN; MONOPHENOL MONOOXYGENASE; OXYGEN; TRYPTOPHAN;

ARTHROPOD; ARTICLE; CALCULATION; EURYPELMA CALIFORNICUM; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; LOBSTER; NONHUMAN; OLIGOMERIZATION; PANULIRUS INTERRUPTUS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION;

ABSORPTION; ANIMALS; ARTHROPODS; BIOSENSING TECHNIQUES; ENERGY TRANSFER; HEMOCYANIN; MODELS, MOLECULAR; OXYGEN; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ARTHROPODA; EURYPELMA CALIFORNICUM; PALINURIDAE; PANULIRUS INTERRUPTUS; TARANTULA;

EID: 48949103837     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.06.009     Document Type: Article

References (32)

1. van Holde K.E., and Miller K.I. Hemocyanins. Adv. Protein. Chem. 47 (1995) 1-81
2. van Holde K.E., Miller K.I., and Decker H. Hemocyanins and invertebrate evolution. J. Biol. Chem. 276 (2001) 15563-15566
3. Loewe R. 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. B. 128 (1978) 161-168
4. Magnus K.A., Hazes B., Ton-That H., Bonaventura C., Bonaventura J., and Hol W.G. Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 19 (1994) 302-309
5. Solomon E.I., Chen P., Metz M., Lee S.K., and Palmer A.E. Oxygen binding, activation, and reduction to water by copper proteins. Angew. Chem. Int. Ed. Engl. 40 (2001) 4570-4590
6. Solomon E.I., Sundaram U.M., and Machonkin T.E. Multicopper oxidases and oxygenases. Chem. Rev. 96 (1996) 2563-2606
7. Richey B., Decker H., and Gill S.J. A direct test of the linearity between optical density change and oxygen binding in hemocyanins. In: Wood E.J. (Ed). Life Chemistry Reports: Supplement 1 (1983), Harwood Academic publishers, Chur, London, New York 309-312
8. Shaklai N., and Daniel E. Fluorescence properties of hemocyanin from Levantina hierosolima. Biochemistry 9 (1970) 564-568
9. Jekel P.A., Bak H.J., Soeter N.M., Vereijken J.M., and Beintema J.J. Panulirus interruptus hemocyanin. The amino acid sequence of subunit b and anomalous behaviour of subunits a and b on polyacrylamide gel electrophoresis in the presence of SDS. Eur. J. Biochem. 178 (1988) 403-412
10. Neuteboom B., Jekel P.A., and Beintema J.J. Primary structure of hemocyanin subunit c from Panulirus interruptus. Eur. J. Biochem. 206 (1992) 243-249
11. Gaykema W.P.J., Hol W.G.J., Vereijken J.M., Soeter N.M., Bak H.J., and Beintema J.J. 3.2 A structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309 (1984) 23-29
12. Volbeda A., and Hol W.G. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution. J. Mol. Biol. 209 (1989) 249-279
13. Markl J., Kempter B., Linzen B., Bijlholt M.M., and van Bruggen E.F. 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
14. de Haas F., and van Bruggen E.F. The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum. A tentative mechanism for cooperative behavior. J. Mol. Biol. 237 (1994) 464-478
15. Decker H., Hartmann H., Sterner R., Schwarz E., and Pilz I. Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin. FEBS Lett. 393 (1996) 226-230
16. Hartmann H., and Decker H. All hierarchical levels are involved in conformational transitions of the 4 × 6-meric tarantula hemocyanin upon oxygenation. Biochim. Biophys. Acta 1601 (2002) 132-137
17. van Heel M., and Dube P. Quaternary structure of multimeric arthropod hemocyanins. Micron 25 (1994) 387-418
18. Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., and Hol W.G. 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
19. Voit R., Feldmaier-Fuchs G., Schweikardt T., Decker H., and Burmester T. 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. Erker W., Hübler R., and Decker H. Structure-based calculation of multi-donor multi-acceptor fluorescence resonance energy transfer in the 4 × 6-mer tarantula hemocyanin. Eur. Biophys. J. 33 (2004) 386-395
21. Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
22. Kuiper H.A., Gaastra W., Beintema J.J., van Bruggen E.F., Schepman A.M., and Drenth J. Subunit composition, X-ray diffraction, amino acid analysis and oxygen binding behaviour of Panulirus interruptus hemocyanin. J. Mol. Biol. 99 (1975) 619-629
23. Lakowicz J.R. Principles of Fluorescence Spectroscopy. 2 ed. (2007), Kluwer Academic/Plenum Publisher, New York
24. Erker W., Beister U., and Decker H. Cooperative transition in the conformation of 24-mer tarantula hemocyanin upon oxygen binding. J. Biol. Chem. 280 (2005) 12391-12396
25. Linzen B., Soeter N.M., Riggs A.F., Schneider H.J., Schartau W., Moore M.D., Yokota E., Behrens P.Q., Nakashima H., Takagi T., et al. The structure of arthropod hemocyanins. Science 229 (1985) 519-524
26. Burmester T. Molecular evolution of the arthropod hemocyanin superfamily. Mol. Biol. Evol. 18 (2001) 184-195
27. Decker H., and Tuczek F. Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends. Biochem. Sci. 25 (2000) 392-397
28. Jaenicke E., and Decker H. Tyrosinases from crustaceans form hexamers. Biochem. J. 371 (2003) 515-523
29. Sanchez-Ferrer A., Rodriguez-Lopez J.N., Garcia-Canovas F., and Garcia-Carmona F. Tyrosinase: a comprehensive review of its mechanism. Biochim. Biophys. Acta 1247 (1995) 1-11
30. Decker H., Schweikardt T., and Tuczek F. The first crystal structure of tyrosinase: all questions answered?. Angew. Chem. Int. Edit. 45 (2006) 4546-4550
31. Erker W., Schoen A., Basché T., and Decker H. Fluorescence labels as sensors for oxygen binding of arthropod hemocyanins. Biochem. Biophys. Res. Commun. 324 (2004) 893-900
32. Zauner G., Strianese M., Bubacco L., Aartsma T.J., Tepper A.W.J.W., and Canters G.W. Type-3 copper proteins as biocompatible and reusable oxygen sensors. Inorg. Chim. Acta 361 (2008) 1116-1121