Functional evaluation of heme vinyl groups in myoglobin with symmetric protoheme isomers

Biochemistry

Volumn 43, Issue 41, 2004, Pages 13149-13155

  Mie, Yasuhiro ^a,d   Yamada, Chiho ^a   Hareau, Georges P J ^a   Neya, Saburo ^b   Uno, Tadayuki ^a   Funasaki, Noriaki ^c   Nishiyama, Katsuhiko ^a   Taniguchi, Isao ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b CHIBA UNIVERSITY   (Japan)

^c KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

^d NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER; NATURAL FREQUENCIES; RAMAN SCATTERING; REDOX REACTIONS; SIGNAL PROCESSING; THERMAL EFFECTS; ULTRAVIOLET RADIATION;

ELECTRON TRANSFER; OXYGEN BINDING; REDOX POTENTIALS; THERMAL DENATURATION;

HEMODYNAMICS;

HEME; HEME DERIVATIVE; MYOGLOBIN;

ARTICLE; DENATURATION; ELECTRON TRANSPORT; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RAMAN SPECTROMETRY; TEMPERATURE; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CIRCULAR DICHROISM; ELECTROCHEMISTRY; ELECTRON TRANSPORT; HEME; HORSES; KINETICS; MYOGLOBIN; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN; STEREOISOMERISM; VINYL COMPOUNDS;

EID: 5444246036     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049051p     Document Type: Article

References (38)

1. La Mar, G. N., Davis, N. L., Parish, D. W., and Smith, K. M. (1983) Heme orientational disorder in reconstituted and native sperm whale myoglobin, J. Mol. Biol. 168, 887-896.
2. La Mar, G. N., Toi, H., and Krisshnamoorthi, R. (1984) Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: evidence for intramolecular reorientation about a heme twofold axis, J. Am. Chem. Soc. 106, 6395-6401.
3. Livingstone, D. J., Davis, L. N., La Mar, G. N., and Brown, W. D. (1984) Influence of heme orientation on oxygen affinity in native sperm whale myoglobin, J. Am. Chem. Soc. 106, 3025-3026.
4. Light, W. R., Rohlfs, R. J., Palmer, G., and Olson, J. S. (1987) Functional effects of heme orientational disorder in sperm whale myoglobin, J. Biol. Chem. 262, 46-52.
5. Neya, S., Nakamura, M., Imai, K., Hori, H., and Funasaki, N. (1996) Functional comparison of the myoglobins reconstituted with symmetric deuterohemes, Biochim. Biophys. Acta 1296, 245-249.
6. Hareau, G. P.-J., Neya, S., Funasaki, N., and Taniguchi, I. (2002) New route to protoporphyrins III and XIII from common starting pyrroles, Tetrahedron Lett. 43, 3109-3111.
7. Taniguchi, I. (1997) Probing metalloproteins and bioelectrochemical systems, Interface 4, 34-37.
8. Hawkridge, F. M., and Taniguchi, I. (1995) The direct electron transfer reactions of cytochrome c at electrode surfaces, Comments Inorg. Chem. 17, 163-187.
9. Armstrong, F. A. (1990) Probing metalloproteins by voltammetry, in Structure and Bonding (Clarke, M. J., Goodenough, J. B., Ibers, J. A., Jorgensen, C. K., Mingos, D. M. P., Neilands, J. B., Palmer, G. A., Reinen, D., Sadler, P. J., Weiss, R., and Williams, R. J. P., Eds.) Vol. 72, pp 137-221, Springer-Verlag, Berlin.
10. Battistuzzi, G., Borsari, M., Loschi, L., Ranieri, A., Sola, M., Mondovi, B., and Marchesini, A. (2001) Redox properties and acid-base equilibria of zucchini mavicyanin, J. Inorg. Biochem. 83, 223-227.
11. Barker, P. D., Gleria, K. Di., Hill, H. A., and Lowe, V. J. (1990) Electron transfer reactions of metalloproteins at peptide-modified gold electrodes, Eur. J. Biochem. 190, 171-175.
12. Dyke, B. R. V., Saltman, P., and Armstrong, F. A. (1996) Control of myoglobin electron-transfer rates by the distal (nonbound) histidine residue, J. Am. Chem. Soc. 118, 3490-3492.
13. Cohen, D. J., King, B. C., and Hawkridge, F. M. (1998) Spectroelectrochemical and electrochemical determination of ligand binding and electron transfer properties of myoglobin, cyanomyoglobin, and imidazolemyoglobin, J. Electroanal. Chem. 447, 53-62.
14. Mie, Y., Sonoda, K., Neya, S., Funasaki, N., and Taniguchi, I. (1998) Electrochemistry of myoglobins reconstituted with azahemes and mesohemes, Bioelectrochem. Bioenerg. 46, 175-184.
15. Taniguchi, I., Sonoda, K., and Mie, Y. (1999) Electroanalytical chemistry of myoglobin with modification of distal histidine by cyanated imidazole, J. Electroanal. Chem. 468, 9-18.
16. Mie, Y., Sonoda, K., Kishita, M., Krestyn, E., Neya, S., Funasaki, N., and Taniguchi, I. (2000) Effect of rapid heme rotation on electrochemistry of myoglobin, Electrochim. Acta 45, 2903-2909.
17. Hardman, K. D., Eylar, E. H., Ray, D. K., Banaszak, L. J., and Gurd, F. R. N. (1966) Isolation of sperm whale myoglobin by low temperature fractionation with ethanol and metallic ions, J. Biol. Chem. 241, 432-442.
18. Hapner, K. D., Bradshaw, R. A., Hartzell, C. R., and Gurd, F. R. N. (1968) Comparison of myoglobins from harbor seal, porpoise, and sperm whale: I. preparation and characterization, J. Biol. Chem. 243, 683-689.
19. Antonini, E., and Brunori, M. (1971) Hemoglobin and myoglobin in Their Reactions with Ligands, pp 19 and 44, North Holland, Amsterdam.
20. Chang, C. K., Dinello, R. K., and Dolphin D. (1989) Iron porphyrins, Inorg. Synth. 20, 147-151.
21. Fuhrhope, J. H., and Smith, K. M. (1975) Hydrolysis of esters, Porphyrins Metalloporphyrins 836-837.
22. Teale, F. W. J. (1959) Cleavage of heam-protein link by acid methylethylketone, Biochim. Biophys. Acta 35, 543.
23. Asakura, T. (1978) Hemoglobin porphyrin modification, Methods Enzymol. 52, 447-455.
24. Ward, B., and Chang, C. K. (1982) A convenient photochemical method for reduction of ferric hemes, Photochem. Photobiol. 35, 757-759.
25. Morikis, D., Champion, P. M., Springer, B. A., Egeberg, K. D., and Sligar, S. G. (1990) Resonance Raman studies of iron spin and axial coordination in distal pocket mutants of ferric myoglobin, J. Biol. Chem. 265, 12143-12145.
26. Kitagawa, T., Kyogoku, Y., Iizuka, T., and Saito, M. I. (1976) Nature of iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering, J. Am. Chem. Soc. 98, 5169-5173.
27. Uno, T., Sakamoto, R., Tomisugi, Y., Ishikawa, Y., and Wilkinson, A. J. (2003) Inversion of axial coordination in myoglobin to create a proximal ligand binding pocket, Biochemistry 42, 10191-10199.
28. Peterson, E. S., Friedman, J. M., Chien, E. Y. T., and Sligar, S. G. (1998) Functional implications of the proximal hydrogen-bonding network in myoglobin: A resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants, Biochemistry 37, 12301-12319.
29. Hu, S., Smith, K. M., and Spiro, T. G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin, J. Am. Chem. Soc. 118, 12638-12646.
30. Hsu, M.-C., and Woody, R. W. (1971) The origin of the heme Cotton effects in myoglobin and hemoglobin, J. Am. Chem. Soc. 93, 3515-3525.
31. Santucci, R., Ascoli, F., La Mar, G. N., Parish, D. W., and Smith, K. M. (1990) Horse heart myoglobin reconstituted with a symmetrical heme: a circular dichroism study, Biophys. Chem. 37, 251-255.
32. Crumpton, M. J., and Polson, A. (1965) A comparison of the conformation of sperm whale metmyoglobin with that of apomyoglobin, J. Mol. Biol. 11, 722-729.
33. Bellelli, A., Antonini, G., Brunori, M., Springer, B. A., and Sligar, S. G. (1990) Transient spectroscopy of the reaction of cyanide with ferrous myoglobin: effect of distal side residues, J. Biol. Chem. 265, 18898-18901.
34. Marzocchi, M., and Smulevich, G. (2003) Relationship between heme vinyl conformation and the protein matrix in peroxidases, J. Roman Spectrosc. 34, 725-736.
35. 5 electron transfer, J. Am. Chem. Soc. 108, 8197-8201.
36. Perutz, M. F. (1976) Structure and mechanism of haemoglobin, Br. Med. Bull. 32, 195-208.
37. Satterlee, J. D., and Erman, J. E. (1983) Temperature and pH dependence of the proton magnetic hyperfine resonance of cytochrome c peroxidase-cyanide, J. Biol. Chem. 258, 1050-1056.
38. Neya, S., Funasaki, N., Shiro, Y., Iizuka, T., and Imai, K. (1994) Consequence of rapid heme rotation to the oxygen binding of myoglobin, Biochim. Biophys. Acta 1208, 31-37.