Myoglobin with modified tetrapyrrole chromophores: Binding specificity and photochemistry

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 7, 2006, Pages 750-763

  Pröll, Stephanie ^a   Wilhelm, Brigitte ^a   Robert, Bruno ^b   Scheer, Hugo ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b CNRS   (France)

Author keywords

Chlorophyll, transmetalated; Myoglobin binding site; Photochemistry; Photodynamic therapy; Stereochemistry, photosynthesis

Indexed keywords

BACTERIOCHLORIN; BACTERIOCHLOROPHYLL; EPIMERASE; MYOGLOBIN; PHEOPHORBIDE; PHYCOCYANOBILIN; PHYTOL; PIGMENT; PROTEIN; TETRAPYRROLE DERIVATIVE; UNCLASSIFIED DRUG; ZINC;

AQUEOUS SOLUTION; ARTICLE; CHROMATOPHORE; COMPARATIVE STUDY; HYDROPHOBICITY; OXIDATION REDUCTION REACTION; PHOTOACTIVATION; PHOTOCHEMISTRY; PHOTOOXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; STEREOCHEMISTRY;

APOPROTEINS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; MODELS, MOLECULAR; MYOGLOBIN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOTOCHEMISTRY; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN; TETRAPYRROLES; ZINC;

EQUUS CABALLUS;

EID: 33746697712     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.03.026     Document Type: Article

References (73)

1. Dickerson R.E., Kendrew J.C., and Strandberg B.E. The crystal structure of myoglobin: phase determination to a resolution of 2 A. by the method of isomorphous replacement. Acta Crystallogr. 14 (1961) 1188-1195
2. Perutz M.F., Muirhead H., Cox J.M., and Goaman L.C.G. Three-dimensional Fourier synthesis of horse oxyhemoglobin at 2.8 A. resolution: the atomic model. Nature 219 (1968) 131-139
3. Schlichting I., and Chu K. Trapping intermediates in the crystal: ligand binding to myoglobin. Curr. Opin. Struck. Biol. 10 (2000) 744-752
4. Frank J., and Schlichting I. Special issue: time-resolved imaging of macromolecular processes and interactions. J. Struct. Biol. 147 3 (2004)
5. Ostermann A., Waschipky R., Parak F.G., and Nienhaus G.U. Ligand binding and conformational motions in myoglobin. Nature 404 (2000) 205-208
6. Schmidt M., Rajagopal S., Ren Z., and Moffat K. Application of singular value decomposition to the analysis of time-resolved macromolecular X-ray data. Biophys. J. 84 (2003) 2112-2129
7. V. Srajer, T. Teng, T. Ursby, B. Perman, D. Bourgeois, C. Pradervand, F. Schotte, R. Kort, Z. Ren, W. Royer, K. Hellingwerf, M. Wulff, K Moffat, NS time-resolved X-ray diffraction studies of structural changes in biological macromolecules. Book of Abstracts, 216th ACS National Meeting, Boston, August 23-27, PHYS-390 (1998).
8. Chen X., Discher B.M., Pilloud D.L., Gibney B.R., Moser C.C., and Dutton P.L. De novo design of a cytochrome b maquette for electron transfer and coupled reactions on electrodes. J. Phys. Chem., B 106 (2002) 617-624
9. Robertson D.E., Farid R.S., Moser C.C., Urbauer J.L., Mulholland S.E., Pidikiti R., Lear J.D., Wand A.J., Degrado W.F., and Dutton P.L. Design and synthesis of multi-haem proteins. Nature 368 (1994) 425-431
10. Rau H.K., and Haehnel W. Design, synthesis, and properties of a novel cytochrome b model. J. Am. Chem. Soc. 120 (1998) 468-476
11. Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science (1991) 1598-1603
12. Parak F.G. Proteins in action: the physics of structural fluctuations and conformational changes. Curr. Opin. Struck. Biol. 13 (2003) 552-557
13. Schlichter J., Friedrich J., Parbel M., and Scheer H. New concepts in spectral diffusion physics of proteins. Photonics Sci. News 6 (2000) 100-111
14. Katz J.J., Shipman L.L., Cotton T.M., and Janson T.R. Chlorophyll aggregation: coordination interactions in Chlorophyll monomers, dimers and oligomers. In: Dolphin D. (Ed). The Porphyrins (1978), Academic Press, New York 402-458 Vol.
15. Ponkratov V.V., Friedrich J., Markovic D., Scheer H., and Vanderkooi J.M. Spectral diffusion experiment with a denatured protein. J. Phys. Chem., B 108 (2004) 1109-1114
16. Moog R.S., Kuki A., Fayer M.D., and Boxer S.G. Excitation transport and trapping in a synthetic Chlorophyllide substituted hemoglobin: orientation of the Chlorophyll S1 transition dipole. Biochemistry 23 (1984) 1564-1571
17. Boxer S.G., Kuki A., Wright K.A., Katz B.A., and Xuong N. Oriented properties of the chlorophylls - electronic absorption-spectroscopy of orthorhombic pyrochlorophyllide alpha-apomyglobin single-crystals. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 1121-1125
18. Pearlstein R.M., Davis R.C., and Ditson S.L. Giant circular dichroism of high molecular-weight chlorophyllide-apomyoglobin complexes. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 400-402
19. Davis R.C., and Pearlstein R.M. Chlorophyllin-apomyoglobin complexes. Nature 280 (1979) 413-415
20. Marko H., Müller N., and Falk H. Complex formation between biliverdin and apomyoglobin. Monatsh. Chem. 120 (1989) 591-595
21. Blauer G. Complexes of bilirubin with proteins. Biochim. Biophys. Acta 884 (1986) 602-604
22. Falk H., Marko H., Muller N., Schmitzberger W., and Stumpe H. Reconstitution of apomyoglobin with bile pigments. Monatsh. Chem. 121 (1990) 893-901
23. Falk H., Marko H., Muller N., and Schmitzberger W. The apomyoglobin heme pocket as a reaction vessel in bile pigment chemistry. Monatsh. Chem. 121 (1990) 903-908
24. Marko H., Müller N., and Falk H. Nuclear-magnetic-resonance investigations of the biliverdin-apomyoglobin complex. Eur. J. Biochem. 193 (1990) 573-580
25. Wagner U.G., Müller N., Schmitzberger W., Falk H., and Kratky C. Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution. J. Mol. Biol. 247 (1995) 326-337
26. In: Moser J.G. (Ed). Photodynamic Tumor Therapy: 2nd and 3rd Generation Photosensitizers (1998), OPA, Amsterdam
27. A,B von Photosynthetischen Reaktionszentren aus Rhodobacter sphaeroides R26: Pigmentsynthese, Pigmentaustausch und Spektroskopie., Dissertation, Universität München (1990).
28. Hartwich G., Fiedor L., Simonin I., Cmiel E., Schaefer W., Noy D., Scherz A., and Scheer H. Metal-substituted bacteriochlorophylls. 1. Preparation and influence of metal and coordination on spectra. J. Am. Chem. Soc. 120 (1998) 3675-3683
29. Omata T., and Murata N. Preparation of chlorophyll a, chlorophyll b and bacteriochlorophyll a by column chromatography with DEAE-Sepharose CL-6B and Sepharose CL-6B. Plant Cell Physiol. 24 (1983) 1093-1100
30. M. Helfrich, Chemische Modifikation Von Chlorophyll-Vorstufen und Deren Verwendung zur Charakterisierung von Enzymen der Chlorophyll-Biosynthese, Dissertation, Ludwig-Maximilians-Universität, Munchen, 1995.
31. Helfrich M., Schoch S., Schäfer W., Ryberg M., and Rudiger W. Absolute configuration of protochlorophyllide alpha and substrate specificity of NADPH-protochlorophyllide oxidoreductase. J. Am. Chem. Soc 118 (1996) 2606-2611
32. Schaber P.M., Hunt J.E., Fries R., and Katz J.J. High-performance liquid-chromatography study of the Chlorophyll allomerization reaction. J. Chromatogr. 316 (1984) 25-41
33. 2-hydroxy-bacteriochlorophyll. FEBS Lett. 261 (1990) 385-388
34. L. Fiedor, Modified Chlorophylls As Models for Primary Photosynthesis and Photosensitizers for Photodynamic Therapy of Cancer., Dissertation, Weizmann Institute of Science, Rehovot, 1994.
35. 1-Cys-á84-phycoviolobilin chromophore of phycoerythrocyanin. Biochemistry 40 (2001) 12444-12456
36. Teale F.W.J. Cleavage of the haem-protein link by acid methylethlyketone. Biochim. Biophys. Acta 35 (1959) 543
37. Wright K.A., and Boxer S.G. Solution properties and synthetic chlorophyllide-apomyoglobin and bacteriochlorophyllide-apomyoglobin complexes. Biochemistry 20 (1981) 7546-7556
38. Mazaki H., and Watanabe T. Self-catalyzed epimerization of Chlorophyll a/a' in organic solvents. Biochim. Biophys. Acta 1016 (1990) 190-196
39. Maurus R., Bogumil R., Nguyen N.T., Mauk A.G., and Brayer G. Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64 → Thr variant. Biochem. J. 332 (1998) 67-74
40. Boxer S.G., and Wright K.A. Preparation and properties of a chlorophyllide-apomyoglobin complex. J. Am. Chem. Soc 101 (1979) 6791-6794
41. H. Snigula, (Bacterio)Chlorophyll-Modifikationen zur Einlagerung in Synthetische Peptide, Dissertation, Ludwig-Maximilians-Universität, Munchen, 2004.
42. Falk H. The Chemistry of Linear Oligopyrroles and Bile Pigments (1989), Springer, Wien, New York
43. Scheer H., and Katz J.J. Nuclear magnetic resonance spectroscopy of porphyrins and metalloporphyrins. In: Smith K.M. (Ed). Porphyrins and Metalloporphyrins (1975), Elsevier, New York 399-524
44. Näveke A., Lapouge K., Sturgis J.N., Harwich G., Simonin I., Scheer H., and Robert B. Resonance Raman spectroscopy of metal-substituted bacteriochlorophylls: characterization of Raman bands sensitive to bacteriochlorin conformation. J. Raman Spectrosc. 28 (1997) 599-604
45. Lapouge K., Näveke A., Sturgis J.N., Hartwich G., Renaud D., Simonin I., Lutz M., Scheer H., and Robert B. Non-bonding molecular factors influencing the stretching wavenumbers of the conjugated carbonyl groups of bacteriochlorophyll a. J. Raman Spectrosc. 29 (1998) 977-981
46. Feiler U., Mattioli T., Katheder I., Scheer H., Lutz M., and Robert B. Effects of vinyl substitutions on resonance Raman spectra of (Bacterio)chlorophylls. J. Raman Spectrosc. 25 (1994) 365-370
47. Smith J.R.L., and Calvin M. Studies on the chemical and photochemical oxidation of Bacteriochlorophyll. J. Am. Chem. Soc. 88 (1966) 4500-4506
48. Griffiths W.T. Protochlorophyllide Photoreduction. In: Scheer H. (Ed). Chlorophylls (1991), CRC, Boca Raton 433-450
49. Vojtechovsky J., Chu K., Berendzen J., Sweet R.M., and Schlichting I. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77 (1999) 2153-2174
50. Bollivar D.W. Intermediate steps in chlorophyll biosynthesis: methylation and cyclization. In: Kadish K.M., Smith K.M., and Guilard R. (Eds). The Porphyrin Handbook. Chlorophylls and Bilins: Biosynthesis, Synthesis and Degradation vol. 13 (2002), Academic press, Amsterdam 49-70
51. Akiyama M., Miyashita H., Kise H., Watanabe T., Miyachi S., and Kobayashi M. Detection of chlorophyll d' and pheophytin a in a chlorophyll d- dominating oxygenic photosynthetic prokaryote Acaryochloris marina. Anal. Sci. 17 (2001) 205-208
52. Maeda H., Watanabe T., Kobayashi M., and Ikegami I. Presence of two Chlorophyll a' I. Molecules at the core of photosystem. Biochim. Biophys. Acta 1099 (1992) 74-80
53. Kobayashi M., Vandemeent E.J., Erkelens C., Amesz J., Ikegami I., and Watanabe T. Bacteriochlorophyll g epimer as a possible reaction center component of Heliobacteria. Biochim. Biophys. Acta 1057 (1991) 89-96
54. Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., and Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5A resolution. Nature 411 (2001) 909-917
55. Mazaki H., Watanabe T., Takahashi T., Struck A., and Scheer H. Epimerization of chlorophyll derivatives. V. Effects of the central magnesium and ring substituents on the epimerization of chlorophyll derivatives. Bull. Chem. Soc. Jpn. 65 (1992) 3080-3087
56. Nakamura A., Akai M., Yoshida E., Taki T., and Watanabe T. Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in Photosystem I of oxygenic photosynthetic organisms. Universal existence of one chlorophyll a' I. molecule in Photosystem. Eur. J. Biochem. 270 (2003) 2446-2458
57. Buchler J.W. Static coordination chemistry of metalloporphyrins. In: Smith K.M. (Ed). Porphyrins and Metalloporphyrins (1975), Elsevier, Amsterdam 157-232
58. Stolzenberg A.M., Schussel L.J., Summers J.S., Foxman B.M., and Petersen J.L. Structures of the homologous series of square-planar metallotetrapyrroles palladium(II) octaethylporphyrin, palladium(II) trans-octaethylchlorin, and palladium(II) tct-octaethylisobacteriochlorin. Inorg. Chem. 31 (1992) 1678-1686
59. Kirmaier C., Gaul D., Debey R., Holten D., and Schenck C.C. Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin. Science 251 (1991) 922-927
60. A. Brandis, Y. Salomon, and A. Scherz, Chlorophyll sensitizers in photodynamic therapy, in: Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications in: B. Grimm, Porra R., Rudiger, W. Rüdiger, H. Scheer Springer, Berlin, 2006, pp. 461-483.
61. A. Brandis, Y. Salomon, A. Scherz, Bacteriochlorophyll sensitizers in photodynamic therapy, in: Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications (B. Grimm, R. Porra, W. Rüdiger, H. Scheer, (Eds.), Springer, Berlin, 2006, pp. 485-494.
62. Spikes J.D., and Bommer J.C. Chlorophyll and related pigments as photosensitizers in biology and medicine. In: Scheer H. (Ed). Chlorophylls (1991), CRC Press, Boca Raton, FL 1181-1204
63. Rosenbach-Belkin V., Chen L., Fiedor L., Tregub I., Pavlotsky F., Brumfeld V., Salomon Y., and Scherz A. Serine conjugates of chlorophyll and bacteriochlorophyll: photocytotoxicity in vitro and tissue distribution in mice bearing melanoma tumors. Photochem. Photobiol. 64 (1996) 174-181
64. Tregub I., Schoch S., Erazo S., and Scheer H. Red-light induced photoreactions of chlorophyll a mixtures with all trans- or 9-cis-β-carotene. J. Photochem. Photobiol. C 98 (1996) 51-58
65. Fiedor J., Fiedor L., Kammhuber N., Scherz A., and Scheer H. Photodynamics of the bacteriochlorophyll-caroteinoid system. 2. Influence of central metal, solvent and β-carotene on photobleaching of bacteriochlorophyll derivatives. Photochem. Photobiol. 76 (2002) 145-152
66. Fiedor J., Fiedor L., Winkler J., Scherz A., and Scheer H. Photodynamics of the bacteriochlorophyll-caroteinoid system. 1. Bacteriochlorophyll-photosensitized oxygenation of β-carotene in acetone. Photochem. Photobiol. 74 (2001) 64-71
67. L. Limantara, P. Köhler, B. Wilhelm, R.J. Porra, H. Scheer, Photostability of Bacteriochlorophyll a and Derivatives Used as Sensitizers for Photodynamic Tumor Therapy. Photochem. Photobiol. ISSN 0031-8655 (Print).
68. Krasnovskii A.A. Reversible photochemical reduction of chlorophyll by ascorbic acid. Dokl. Akad. Nauk SSSR 60 (1948) 421-424
69. Scheer H., and Katz J.J. Structure of the Krasnovskii photoreduction product of chlorophyll a. Proc. Natl. Acad. Sci. U.S.A. 71 (1974) 1626-1629
70. Fiedor J., Fiedor L., Haessner R., and Scheer H. Stable mono- and di-endoperoxides of β-carotene as products of photosensitized oxygenation. Biochim. Biophys. Acta 1709 (2005) 1-4
71. Collman J.P., and Zhang X. Functional analogs of the oxygen binding and activating heme proteins. Comprehensive Supramolecular Chemistry vol. 5 (1996) 1-32
72. Drzewiecka-Matuszek A., Skalna A., Karocki A., Stochel G., and Fiedor L. Effects of heavy central metal on the ground and excited states of chlorophyll. J. Biol. Inorg. Chem. 10 (2005) 453-462
73. Moss G.P. IUPAC-IUB Joint commission biochemical nomenclature (JCBN). Nomenclature of Tetrapyrroles. Recommendation 1986. Eur. J. Biochem. 178 (1988) 277-328