Structure-based calculation of multi-donor multi-acceptor fluorescence resonance energy transfer in the 4×6-mer tarantula hemocyanin

European Biophysics Journal

Volumn 33, Issue 5, 2004, Pages 386-395

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

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Fluorescence quenching; FRET; Oxygen binding; Tarantula hemocyanin; Tryptophan

Indexed keywords

COPPER COMPLEX; HEMOCYANIN; TRYPTOPHAN;

ARTHROPOD; ARTICLE; CALCULATION; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; FLUORESCENCE RESONANCE ENERGY TRANSFER; OXYGEN AFFINITY; QUANTUM MECHANICS; SPECTROSCOPY; SPIDER; STRUCTURE ANALYSIS; TARANTULA;

ARANEAE; ARTHROPODA; DECAPODA (CRUSTACEA); EURYPELMA CALIFORNICUM; LIMULUS POLYPHEMUS; MEROSTOMATA; MOLLUSCA; POLYPHEMUS;

EID: 4143082538     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-003-0371-2     Document Type: Article

References (39)

1. Baldwin MJ, Root DE, Pate JE, Fujisawa K, Kitajima N, Solomon EI (1992) 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 114:10421-10431
2. Boteva R, Ricchelli F, Sartor G, Decker H (1993) Fluorescence properties of hamocyanin from tarantula (Eurypelma californicum): a comparison between the whole molecule and isolated subunits. J Photochem Photobiol B 17:145-153
3. Burmester T (2001) Molecular evolution of the arthropod hemocyanin superfamily. Mol Biol Evol 18:184-195
4. b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol 278:113-150
5. Chen RF (1967) Fluorescence quantum yields of tryptophan and tyrosine. Anal Lett 1:35-42
6. Cuff ME, Miller KI, van Holde KE, Hendrickson WA (1998) Crystal structure of a functional unit from Octopus hemocyanin. J Mol Biol 278:855-870
7. Decker H, Hartmann H, Sterner R, Schwarz E, Pilz I (1996) Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin. FEBS Lett 393:226-230
8. De Haas F, Van Bruggen EF (1994) The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum. A tentative mechanism for cooperative behavior. J Mol Biol 237:464-478
9. Dewey TG, Hammes GG (1980) Calculation of fluorescence resonance energy transfer on surfaces. Biophys J 32:1023-1036
10. Dos Remedios CG, Moens PDJ (1995) Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. J Struct Biol 115:175-185
11. Fairclough RH, Cantor CR (1978) The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol 48:347-379
12. Floyd JS, Haralampus-Grynaviski N, Ye T, Zheng B, Simon JD, Edington MD (2001) Time-resolved spectroscopic studies of radiationless decay processes in photoexcited hemocyanins. J Phys Chem B 105:1478-1483
13. Förster T (1948) Zwischenmolekulare energiewanderung und fluoreszenz. Ann Phys 2:55-75
14. Gaykema WPJ, Hol WGJ, Vereijken JM, Soeter NM, Bak HJ, Beintema JJ (1984) 3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin. Nature 309:23-29
15. Hartmann H, Decker H (2002) All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation. Biochim Biophys Acta 1601:132-137
16. Hazes B, Magnus KA, Bonaventura C, Bonaventura J, Dauter Z, Kalk KH, Hol WGJ (1993) Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: clues for a mechanism for allosteric regulation. Protein Sci 2:597-619
17. 2). J Am Chem Soc 111:8975-8976
18. 2) (R = i-Pr and Ph). J Am Chem Soc 114:1277-1291
19. Lakowicz JR (1999) Principles of fluorescence spectroscopy, 2nd edn. Kluwer/Plenum, New York
20. Linzen B, Soeter NM, Riggs AF, Schneider HJ, Schartau W, Moore MD, Yokota E, Behrens PQ, Nakashima H, Takagi T, Nemoto T, Vereijken JM, Bak HJ, Beintema JJ, Volbeda A, Gaykema WPJ, Hol WGJ (1985) The structure of arthropod hemocyanins. Science 229:519-524
21. Loewe R (1978) 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 128:161-168
22. Magnus KA, Hazes B, Ton-That H, Bonaventura C, Bonaventura J, Hol WG (1994) Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins 19:302-309
23. Markl J, Decker H (1992) Molecular structure of the arthropod hemocyanins. Adv Comp Environ Physiol 13:325-375
24. Markl J, Kempter B, Linzen B, Bijholt MMC, Van Bruggen EFJ (1981) Hemocyanins in spiders, XVI[1]. Subunit topography and a model of the quaternary structure of Eurypelma hemocyanin. Hoppe Seylers Z Physiol Chem 362:1631-1641
25. Perbandt M, Guthohrlein E W, Rypniewski W, Idakieva K, Stoeva S, Voelter W, Genov N, Betzel C (2003) The structure of a functional unit from the wall of a gastropod hemocyanin offers a possible mechanism for cooperativity. Biochemistry 42:6341-6346
26. Ricchelli F, Beltramini M, Flamigni L, Salvato B (1987) Emission quenching mechanisms in Octopus vulgaris hemocyanin: steady state and time-resolved fluorescence studies. Biochemistry 26:6933-6939
27. Richey B, Decker H, Gill SJ (1983) A direct test of the linearity between optical density change and oxygen binding in hemocyanins. In: Wood EJ (ed) Life chemistry reports: supplement 1. Harwood, New York, pp 309-312
28. Salvato B, Beltramini M (1987) Hemocyanins: molecular structure and reactivity of the binuclear copper site. Life Chem Rep 5:249-275
29. Salvato B, Beltramini M (1990) Hemocyanins: molecular architecture, structure and reactivity of the binuclear copper active site. Life Chem Rep 8:1-47
30. Savel-Niemann A, Markl J, Linzen B (1988) Hemocyanins in spiders. XXII. Range of allosteric interaction in a four-hexamer hemocyanin. Co-operativity and Bohr effect in dissociation intermediates. J Mol Biol 204:385-395
31. Shaklai N, Daniel E (1970) Fluorescence properties of hemocyanin from Levantina hierosolima. Biochemistry 9:564-568
32. Shaklai N, Daniel E (1972) Phosphorescence properties of hemocyanin from Levantina hierosolima. Biochemistry 11:2199-2203
33. Stryer L (1978) Fluorescence energy transfer as a spectroscopic ruler. Annu Rev Biochem 47:819-846
34. Van der Meer BW, Coker G, Chen SYS (1994) Resonance energy transfer. VCH, New York
35. Van Heel M, Dube P (1994) Quaternary structure of multihexameric arthropod hemocyanins. Micron 25:387-418
36. Van Holde KE, Miller KI (1995) Hemocyanins. Adv Protein Chem 47:1-81
37. Van Holde KE, Miller KI, Decker H (2001) Hemocyanins and invertebrate evolution. J Biol Chem 276:15563-15566
38. Voit R, Feldmaier-Fuchs G, Schweikardt T, Decker H, Burmester T (2000) Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma californicum. Structure and intramolecular evolution of the subunits. J Biol Chem 275:39339-39344
39. Volbeda A, Hol WG (1989) Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution. J Mol Biol 209:249-279