Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I from Lucina pectinata

Biospectroscopy

Volumn 4, Issue 5, 1998, Pages 311-326

  Silfa, Eilyn ^a   Almeida, Maritza ^a   Cerda, Jose ^a   Wu, Shaoxiong ^b   López Garriga, Juan ^a  

^a UNIVERSITY OF PUERTO RICO   (Puerto Rico)

^b EMORY UNIVERSITY   (United States)

Author keywords

Heme vinyl groups; Hemoglobin I; Hydrogen sulfide; Lucina pectinata

Indexed keywords

CARBON MONOXIDE; CYANIDE; HEME; HEMOGLOBIN; HEMOGLOBIN I, NON MAMMALIAN; HEMOGLOBIN I, NON-MAMMALIAN; HEMOGLOBIN VARIANT; HYDROGEN SULFIDE; PROTON; VINYL DERIVATIVE;

ANIMAL; ARTICLE; BIVALVE; CHEMICAL MODEL; CHEMISTRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; RAMAN SPECTROMETRY;

ANIMALS; BIVALVIA; CARBON MONOXIDE; CYANIDES; HEME; HEMOGLOBINS; HEMOGLOBINS, ABNORMAL; HYDROGEN SULFIDE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; PROTONS; SPECTRUM ANALYSIS, RAMAN; VINYL COMPOUNDS;

EID: 0031615694     PISSN: 10754261     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1520-6343(1998)4:5<311::AID-BSPY3>3.0.CO;2-T     Document Type: Article

References (57)

1. D. W. Kraus and J. B. Wittenberg, "Hemoglobins of Lucina pectinata/bactena symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands," J. Biol. Chem., 265, 16043-16053 (1990).
2. M. Rizzi, J. B. Wittenberg, A. Coda, P. Ascenzi, and M. Bolognesi, "Structural bases for sulfide recognition in Lucina pectinata hemoglobin I," J. Mol. Biol., 258, 1-5 (1996).
3. M. Rizzi, J. B. Wittenberg, A. Coda, M. Fasano, P. Ascenzi, and M. Bolognesi, "Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata," J. Mol. Biol., 244, 86-99 (1994).
4. X. Zhao, K. Vyas, B. D. Nguyen, K. Rajarathnam, G. N. La Mar, T. Li, G. N. Phillips, Jr., R. J. Eich, J. S. Olson, J. Ling, and D. Bocian, "A double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobin," J. Biol. Chem., 270, 20763-20774 (1995).
5. A. M. Navarro, M. Maldonado, J. Gonzales-Lagoa, R. López-Mejia, J. López-Garriga, and J. L. Colón, "Control of carbon monoxide binding states and dynamics in hemoglobin I of Lucina pectinata by nearby aromatic residues," Inorg. Chim. Act., 243, 161-166 (1996).
6. E. Lloyd, D. L. Burk, J. C. Ferrer, R. Maurus, J. Doran, P. R. Carey, G. D. Brayer, and A. G. Mauk, "Electrostatic modification of the active site of myoglobin: Characterization of the proximal Ser92Asp variant," Biochemistry, 35, 11901-11912 (1996).
7. B. A. Springer, S. G. Sligar, J. S. Olson, and G. N. Phillips, "Mechanisms of ligand recognition in myoglobin," Chem. Rev., 94, 699-714 (1994).
8. Y. Yamamoto, A. Ōsawa, Y. Inoue, R. Chûjô, and T. Suzuki, "Determination of the functionally important heme peripheral vinyl group orientation in paramagnetic hemoproteins by 2-D NMR," FEBS LETTS., 247, 263-267 (1989).
9. G. N. La Mar, D. B. Viscio, K. Gersonde, and H. Sick, "Proton nuclear magnetic resonance study of the rotational position and oscillatory mobility of vinyl group in allosteric monomeric insect hemoglobins," Biochemistry, 17, 361-367 (1978).
10. J. D. Satterlee and J. E. Erman, "Temperature and pH dependence of the proton magnetic hyperfine resonances of cytochrome c peroxidase-cyanide," J. Biol. Chem., 258, 1050-1056 (1983).
11. 5 electron transfer," J. Am. Chem. Soc., 108, 8197-8201 (1986).
12. Y. Yamamoto, K. Iwafune, N. Nanai, R. Chûjô, Y. Inoue, and T. Suzuki, "Orientation and mobility of the heme vinyl groups in myoglobins with the aid of NOE and MATDUHM NMR," Biochim. Biophys. Acta, 1120, 173-182 (1992).
13. T. Kitagawa, Y. Ozaki, and Y. Kyogoku, "Resonance Raman studies on the ligand-iron interactions in hemoproteins and metalloproteins," Adv. Biophis., 11, 153-196 (1978).
14. S. A. Asher, "Resonance Raman spectroscopy of hemoglobin," Met. Enzymol., 76, 371-413 (1981).
15. G. T. Babcock, "Raman scattering by cytochrome oxidase and by heme a model compound," in Biological Applications of Raman Spectroscopy, Vol. 3 Chap. 7, Wiley Interscience, New York, 1988.
16. T. G. Spiro, "Resonance Raman spectroscopy as a probe of heme protein structure and dynamics," Adv. Protein Chem., 37, 111-159 (1985).
17. A. J. Sitter, C. M. Reczek, and J. Terner, "Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration," J. Biol. Chem., 260, 7515-7522 (1985).
18. A. Desbois, G. Mazza, F. Stetzkowski, and M. Lutz, "Resonance Raman spectroscopy of protohemeprotein interactions in oxygen-carrying hemoproteins and in peroxidases," Biochim. Biophys. Acta, 785, 161-176 (1984).
19. W. A. Kalsbeck, A. Ghosh, R. K. Pandey, K. M. Smith, and F. D. Bocian, "Determinants of the vinyl stretching frequency in protoporphyrins. Implications for cofactor-protein interactions in heme proteins," J. Am. Chem. Soc., 117, 10959-10968 (1995).
20. K. Gersonde, N. T. Yu, S. H. Lin, K. M. Smith, and D. W. Parish, "Resonance Raman assignment and evidence for noncoupling of individual 2- and 4-vinyl vibrational modes in a monomeric cyanomethemoglobin," Biochem., 28, 3960-3966 (1989).
21. G. Smulevich, A. R. Mantini, M. Paoli, M. Coletta, and G. Geraci, "Resonance Raman studies of the heme active site of the homodimeric myoglobin from Nassa mutabilis: A peculiar case," Biochem., 34, 7507-7516 (1995).
22. K. Wüthrich, NMR of Proteins and Nucleic Acid, Wiley, New York, 1986, pp. 292.
23. 1H NMR studies of pyridine binding to metmyoglobin," Inorg. Chim. Acta., 249, 239-243 (1996).
24. 1H nuclear overhauser effect," J. Am. Chem. Soc., 108, 4244-4245 (1986).
25. S. J. McLachlan, G. N. La Mar, and E. Sletten, "Ferricytochrome b5: Assignment of heme propionate resonances on the basis of nuclear overhauser effect measurements and the nature of interprotein contacts with partner redox proteins," J. Am. Chem. Soc., 108, 1285-1291 (1986).
26. 1H NMR study of the electronic and molecular structure of the heme cavity in horseradish peroxidase. Complete heme resonance assignments based on saturation transfer and nuclear overhauser effects," J. Am. Chem. Soc., 109, 265-272 (1987).
27. 1H NMR resonance assignment and dynamic analysis of phenylalanine CD1 in a low-spin ferric complex of sperm whale myoglobin," J. Am. Chem. Soc., 110, 4176-4182 (1988).
28. 1H NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers," Biochim. Biophys. Acta, 1041, 186-194 (1990).
29. S. D. Emerson and G. N. La Mar, "Solution structural characterization of cyanometmyoglobin: Resonance assignment of heme cavity residues by two dimensional NMR," Biochemistry, 29, 1545-1556 (1990).
30. 1H NMR hyperfine shifts pattern as a probe for ligation state in high-spin ferric hemoproteins: Water binding in metmyoglobin mutants," J. Am. Chem. Soc., 113, 7886-7892 (1991).
31. 1H NMR investigation of the heme cavity of elephant (E7 Gln) met-cyano-myoglobin," J. Biol. Chem., 268, 14826-14835 (1993).
32. 1H NMR probes for the inter-segmental hydrogen bonds in myoglobins," J. Biochem., 120, 126-132 (1996).
33. Y. Yamamoto and T. Suzuki, "NMR study of the active site of shark met-cyano myoglobins," Biochim. Biophys. Acta, 1293, 129-139 (1996).
34. C. L. Hunter, E. Lloyd, L. D. Eltis, S. P. Rafferty, H. Lee, M. Smith, and A. G. Mauk, "Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5," Biochemistry, 36, 1010-1017 (1997).
35. C. Ho and I. M. Russu, "Proton nuclear magnetic resonance investigation of hemoglobin," in Methods in Enzymology, vol. 76, Academic Press, New York, 1981, pp. 275-312.
36. K.-B. Lee, E. Jun, G. N. La Mar, I. Rezzano, R. Pandey, K. M. Smith, F. A. Walker, and D. A. Buttlaire, "Influence of heme vinyl- and carboxilate-protein contacts on structure and redox properties of bovine cytochrome b5," J. Am. Chem. Soc., 113, 3576-3583 (1991).
37. J. S. De Ropp and G. N. La Mar, "2D NMR assignment of hyperfine-shifted resonances in strongly paramagnetic metalloproteins: Resting-state horseradish peroxidase," J. Am. Chem. Soc., 113, 4348-4350 (1991).
38. 1H NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin," Biochim. Biophys. Acta., 832, 175-185 (1985).
39. J. T. J. Lecomte and M. Cocco, "Structural features of the protoporphyrin-apomyoglobin complex: A proton NMR spectroscopy study," Biochemistry, 29, 11057-11067 (1990).
40. D. W. Kraus, J. B. Wittenberg, L. Jing-Fen, and J. Peisach, "Hemoglobin of the Lucina pectinata/ bacteria symbiosis. II. An electron paramagnetic resonance and optical spectral study of the ferric proteins," J. Biol. Chem., 265, 16054-16059 (1990).
41. 15N substituted derivatives. II. A normal coordinate analysis," J. Chem. Phys., 69, 4526-4534 (1978).
42. P. V. Argade, M. Sassaroli, D. L. Rousseau, T. Inubushi, M. Ikeda-Saito, and A. Lapidot, "Confirmation of the assignment of the iron-Histidine stretching mode in myoglobin," J. Am. Chem. Soc., 106, 6593-6596 (1984).
43. S. Kaminaka, T. Ogura, K. Kitagishi, T. Yonetani, and T. Kitagawa, "Resonance Raman spectra of intermediate ligated forms of hemoglobin: The νFe-His, νFe-CO, δFeCO and νOO modes of cross-linked Fe-Co hybrid hemoglobins," J. Am. Chem. Soc., 111, 3787-3794 (1989).
44. S. Choi and T. G. Spiro, "Out-of-plane deformation in the resonance Raman spectra of metalloporphyrins and heme proteins," J. Am. Chem. Soc., 105, 3683-3692 (1983).
45. S. Hu, I. K. Morris, J. P. Singh, K. M. Smith, and T. G. Spiro, "Complete assignment of the resonance Raman spectra of cytochrome c," J. Am. Chem. Soc., 115, 12446-12458 (1993).
46. J. M. Friedman and E. Peterson, "Structure, function and dynamics in hemoglobins and myoglobins: Time resolved and cryogenic resonance Raman studies," XVth International Conference on Raman Spectroscopy, 1996, pp. 428-429.
47. J. F. Gerda, E. Silfa, and J. López-Garriga, "Unusual conformation of the heme propionates in the hydrogen sulfide-binding hemoglobin from Lucina pectinata," Manuscript submitted to J. Am. Chem. Soc., 1998.
48. K. Uchida, Y. Susai, E. Hirotani, T. Kimura, T. Yoneya, H. Takeuchi, and I. Harada, "4-vinyl and 2,4-divinyl deuteration effects on the low frequency resonance Raman bands of myoglobin: Correlation with the structure of vinyl group," J. Biochem., 103, 979-985 (1988).
49. 1H NMR identification of a new aromatic residue in the heme pocket," Biochemistry, 29, 578-2585 (1990).
50. 1H NMR Studies of the Lucina pectinata met-cyano and met-hydrogen sulfide Hemoglobin I complexes," M.S. Thesis, Chemistry Department, University of Puerto Rico, Mayaguez Campus, 1997.
51. S. Ramaprasad, R. D. Johnson, and G. N. La Mar, "Vinyl mobility in myoglobin as studied by time-dependent nuclear overhauser effect measurements," J. Am. Chem. Soc., 106, 3632-3635 (1984).
52. 1H nuclear magnetic resonance determination of hydrogen bonding of the E10(66)Arg side-chain to the bound ligand in Aplisia cyanomet myoglobin," J. Mol. Biol., 224, 891-897 (1992).
53. G. N. La Mar, J. B. Haukson, L. B. Dugad, P. A. Liddell, N. Venkataramana, and K. M. Smith, "Proton NMR study of the heme rotational mobility in myoglobin: The role of propionate salt bridges in anchoring the heme," J. Am. Chem. Soc., 113, 1544-1550 (1991).
54. 1H nuclear magnetic resonance determination of the distal pocket structure of cyanomet complexes of genetically engineered sperm wale myoglobin His64(E7) → Val, Thr67(E10) → Arg. The role of distal hydrogen bonding by Arg67(E10) in modulating ligand tilt," Biophys. J., 65, 2178-2190 (1993).
55. D. H. Peyton, G. N. La Mar, S. Ramaprasad, S. W. Unger, S. Sankar, and K. Gersonde, "Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi cyanomet hemoglobins," J. Mol. Biol., 221, 1015-1026 (1991).
56. G. N. La Mar, N. L. Davis, R. D. Johnson, W. S. Smith, J. B. Hauksson, D. L. Budd, F. Dalichow, K. C. Langry, I. K. Morris, and K. M. Smith, "Nuclear magnetic resonance investigation of the electron structure of deoxymyoglobin," J. Am. Chem. Soc., 115, 3869-3876 (1993).
57. J. Kuriyan, S. Wilz, M. Karplus, and G. A. Petsko, "X-ray structure and refinement of carbon monoxide (Fe II)-myoglobin at 1.5 Å resolution," J. Mol. Biol., 192, 133-154 (1986).