메뉴 건너뛰기




Volumn 43, Issue 13, 2004, Pages 3793-3801

Crystal Structure of Human Heme Oxygenase-1 in a Complex with Biliverdin

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHELATION; COBALT; COMPLEXATION; CONFORMATIONS; CRYSTAL ORIENTATION; CRYSTAL STRUCTURE; SUBSTRATES;

EID: 1842539397     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035451l     Document Type: Article
Times cited : (46)

References (51)
  • 1
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R., Marver, H. S., and Schmid, R. (1969) Microsomal heme oxygenase. Characterization of the enzyme, J. Biol. Chem. 244, 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 0001000615 scopus 로고
    • (Dolphin, D., Ed.) Academic Press, New York
    • Schmid, R., and McDonagh, A. F. (1979) The Porphyrins (Dolphin, D., Ed.) Vol. VI, pp 257-292, Academic Press, New York.
    • (1979) The Porphyrins , vol.6 , pp. 257-292
    • Schmid, R.1    McDonagh, A.F.2
  • 4
    • 0001490181 scopus 로고
    • Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation
    • Drummond, G. S., and Kappas, A. (1981) Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation, Proc. Natl. Acad. Sci. U.S.A. 78, 6466-6470.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6466-6470
    • Drummond, G.S.1    Kappas, A.2
  • 5
    • 0028239795 scopus 로고
    • Free and albumin-bound bilirubin are efficient co-antioxidants for a-tocopherol, inhibiting plasma and low-density lipoprotein lipid peroxidation
    • Neuzil, J., and Stocker, R. (1994) Free and albumin-bound bilirubin are efficient co-antioxidants for a-tocopherol, inhibiting plasma and low-density lipoprotein lipid peroxidation, J. Biol. Chem 269, 16712-16719.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16712-16719
    • Neuzil, J.1    Stocker, R.2
  • 6
    • 0026035905 scopus 로고
    • Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophils cell free-system
    • Kwak, J. Y., Takeshige, K., Cheung, B. S., and Minakami, S. (1991) Bilirubin inhibits the activation of superoxide-producing NADPH oxidase in a neutrophils cell free-system, Biochim. Biophys. Acta 1076, 369-373.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 369-373
    • Kwak, J.Y.1    Takeshige, K.2    Cheung, B.S.3    Minakami, S.4
  • 7
    • 0025637021 scopus 로고
    • Carotenoids, tocopherols and thiols as biological singlet molecular oxygen quenchers
    • Di-Mascio, P., Devasagayam, T. P., Kaiser, S., and Sies, H. (1990) Carotenoids, tocopherols and thiols as biological singlet molecular oxygen quenchers, Biochem. Soc. Trans. 18, 1054-1056.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 1054-1056
    • Di-Mascio, P.1    Devasagayam, T.P.2    Kaiser, S.3    Sies, H.4
  • 8
    • 0024588311 scopus 로고
    • Synergistic interaction between Vitamin E and the bile pigments bilirubin and biliverdin
    • Stocker, R., and Peterhans, E. (1989) Synergistic interaction between Vitamin E and the bile pigments bilirubin and biliverdin, Biochim. Biophys. Acta 1002, 238-244.
    • (1989) Biochim. Biophys. Acta , vol.1002 , pp. 238-244
    • Stocker, R.1    Peterhans, E.2
  • 9
    • 0032169723 scopus 로고    scopus 로고
    • Activation of the Ah receptor signal transduction pathway by bilirubin and biliverdin
    • Phelan, D., Winter, G. M., Rogers, W. J., Lam, J. C., and Denison, M. S. (1998) Activation of the Ah receptor signal transduction pathway by bilirubin and biliverdin, Arch. Biochem. Biophys. 357, 155-163.
    • (1998) Arch. Biochem. Biophys. , vol.357 , pp. 155-163
    • Phelan, D.1    Winter, G.M.2    Rogers, W.J.3    Lam, J.C.4    Denison, M.S.5
  • 11
    • 0032494085 scopus 로고    scopus 로고
    • Heme oxygenase-1-derived carbon monoxide contributes to the suppression of acute hypertensive responses in vivo
    • Motterlini, R., Gonzales, A., Foresti, R., Clark, J. E., Green, C. J., and Winslow, R. M. (1998) Heme oxygenase-1-derived carbon monoxide contributes to the suppression of acute hypertensive responses in vivo, Circ. Res. 83, 568-577.
    • (1998) Circ. Res. , vol.83 , pp. 568-577
    • Motterlini, R.1    Gonzales, A.2    Foresti, R.3    Clark, J.E.4    Green, C.J.5    Winslow, R.M.6
  • 12
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines, M. D. (1997) The heme oxygenase system: A regulator of second messenger gases, Annu. Rev. Pharmacol. Toxicol. 37, 517-554.
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 13
    • 0032897558 scopus 로고    scopus 로고
    • Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes
    • Mireles, L. C., Lum, M. A., and Dennery, P. A. (1999) Antioxidant and cytotoxic effects of bilirubin on neonatal erythrocytes, Pediatr. Res. 45, 355-362.
    • (1999) Pediatr. Res. , vol.45 , pp. 355-362
    • Mireles, L.C.1    Lum, M.A.2    Dennery, P.A.3
  • 15
    • 0033980283 scopus 로고    scopus 로고
    • The heme oxygenase-carbon monoxide system: A regulator of hepatobilary funation
    • Suematsu, M., and Ishimura, Y. (2000) The heme oxygenase-carbon monoxide system: a regulator of hepatobilary funation, Hepatology 31, 3-6.
    • (2000) Hepatology , vol.31 , pp. 3-6
    • Suematsu, M.1    Ishimura, Y.2
  • 16
    • 0028967839 scopus 로고
    • Expression and characterization of truncated human heme oxygenase hHO-1 and a fusion protein of hHO-1 with human cytochrome P450 reductase
    • Wilks, A., Black, S. M., Miller, W. L., and Ortiz de Montellano, P. R. (1995) Expression and characterization of truncated human heme oxygenase hHO-1 and a fusion protein of hHO-1 with human cytochrome P450 reductase, Biochemistry 34, 4421-4427.
    • (1995) Biochemistry , vol.34 , pp. 4421-4427
    • Wilks, A.1    Black, S.M.2    Miller, W.L.3    Ortiz De Montellano, P.R.4
  • 19
    • 0019332526 scopus 로고
    • Oxygenated form of heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex
    • Yoshida, T., Noguchi, M., and Kikuchi, G. (1980) Oxygenated form of heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex, J. Biol. Chem. 255, 4418-4420.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4418-4420
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 20
    • 0033579192 scopus 로고    scopus 로고
    • Hydroperoxy-heme oxygenase generated by cryoreduction catalyzes the formation of α-meso-hydroxyheme as detected by EPR and ENDOR
    • Davydov, R. M., Yoshida, T., Ikeda-Saito, M., and Hoffman, B. M. (1999) Hydroperoxy-heme oxygenase generated by cryoreduction catalyzes the formation of α-meso-hydroxyheme as detected by EPR and ENDOR, J. Am. Chem. Soc. 121, 10656-10657.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10656-10657
    • Davydov, R.M.1    Yoshida, T.2    Ikeda-Saito, M.3    Hoffman, B.M.4
  • 21
    • 0027998288 scopus 로고
    • Heme oxygenase HO-1. Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of α-meso-hydroxyheme
    • Wilks, A., Torpey, J., and Ortiz de Montellano, P. R. (1994) Heme oxygenase HO-1. Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of α-meso-hydroxyheme, J. Biol. Chem. 269, 29553-29556.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29553-29556
    • Wilks, A.1    Torpey, J.2    Ortiz De Montellano, P.R.3
  • 22
    • 0033603348 scopus 로고    scopus 로고
    • Ferric α-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents
    • Sakamoto, H., Omata, Y., Palmer, G., and Noguchi, M. (1999) Ferric α-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents, J. Biol. Chem. 274, 18196-18200.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18196-18200
    • Sakamoto, H.1    Omata, Y.2    Palmer, G.3    Noguchi, M.4
  • 23
    • 0009611092 scopus 로고    scopus 로고
    • Molecular oxygen oxidizes the porphyrin ring of the ferric α-hydroxyheme in heme oxygenase in the absence of reducing equivalents
    • Migita, C. T., Fujii, H., Matera, K. M., Takahashi, S., Zhou, H., and Yoshida, T. (1999) Molecular oxygen oxidizes the porphyrin ring of the ferric α-hydroxyheme in heme oxygenase in the absence of reducing equivalents. Biochim. Biophys. Acta 1432, 203-213.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 203-213
    • Migita, C.T.1    Fujii, H.2    Matera, K.M.3    Takahashi, S.4    Zhou, H.5    Yoshida, T.6
  • 24
    • 0030905395 scopus 로고    scopus 로고
    • Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents
    • Liu, Y., Moënne-Loccoz, P., Loehr, T. M., and Ortiz de Montellano, P. R. (1997) Heme oxygenase-1, intermediates in verdoheme formation and the requirement for reduction equivalents, J. Biol. Chem. 272, 6909-6917.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6909-6917
    • Liu, Y.1    Moënne-Loccoz, P.2    Loehr, T.M.3    Ortiz De Montellano, P.R.4
  • 25
    • 0542422859 scopus 로고    scopus 로고
    • Heme oxygenase mechanism: Evidence for an electrophilic ferric peroxide species
    • Ortiz de Montellano, P. R. (1998) Heme oxygenase mechanism: evidence for an electrophilic ferric peroxide species, Acc. Chem. Res. 31, 543-549.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 543-549
    • Ortiz De Montellano, P.R.1
  • 26
    • 0037062587 scopus 로고    scopus 로고
    • Crystal structure of rat apo-heme oxygenase (HO-1): Mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms
    • Sugishima, M., Sakamoto, H., Kakuta, Y., Omata, Y., Hayashi, S., Noguchi, M., and Fukuyama, K. (2002) Crystal structure of rat apo-heme oxygenase (HO-1): Mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms, Biochemistry 41, 7293-7300.
    • (2002) Biochemistry , vol.41 , pp. 7293-7300
    • Sugishima, M.1    Sakamoto, H.2    Kakuta, Y.3    Omata, Y.4    Hayashi, S.5    Noguchi, M.6    Fukuyama, K.7
  • 28
    • 0346003806 scopus 로고    scopus 로고
    • Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: Implication for regiospecific hydroxylation of heme at the α-meso carbon
    • Sugishima, M., Sakamoto, H., Higashimoto, Y., Omata, Y., Hayashi, S., Noguchi, M., and Fukuyama, K. (2002) Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: implication for regiospecific hydroxylation of heme at the α-meso carbon, J. Biol. Chem. 277, 45086-45090.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45086-45090
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Omata, Y.4    Hayashi, S.5    Noguchi, M.6    Fukuyama, K.7
  • 29
    • 0041355223 scopus 로고    scopus 로고
    • Crystal Structure of Rat Heme Oxygenase-1 in Complex with Biliverdin-Iron Chelate
    • Sugishima, M., Sakamoto, H., Higashimoto, Y., Noguchi, M., and Fukuyama, K. (2003) Crystal Structure of Rat Heme Oxygenase-1 in Complex with Biliverdin-Iron Chelate, J. Biol. Chem. 278, 32352-32358.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32352-32358
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Noguchi, M.4    Fukuyama, K.5
  • 30
    • 0141818003 scopus 로고    scopus 로고
    • Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis: Implications for oxygen activation
    • Friedman, J., Lad, L., Deshmukh, R., Li, H., Wilks, A., and Poulos, T. L. (2003) Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis: Implications for oxygen activation, J. Biol. Chem. 278, 34654-34659.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34654-34659
    • Friedman, J.1    Lad, L.2    Deshmukh, R.3    Li, H.4    Wilks, A.5    Poulos, T.L.6
  • 31
    • 0037709372 scopus 로고    scopus 로고
    • Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: Catalytic implications
    • Lad, L., Wang, J., Li, H., Friedman, J., Bhaskar, B., Ortiz de Montellano, P. R., and Poulos, T. L. (2003) Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications, J. Mol. Biol. 330, 527-538.
    • (2003) J. Mol. Biol. , vol.330 , pp. 527-538
    • Lad, L.1    Wang, J.2    Li, H.3    Friedman, J.4    Bhaskar, B.5    Ortiz De Montellano, P.R.6    Poulos, T.L.7
  • 32
    • 0034734346 scopus 로고    scopus 로고
    • Participation of carboxylate amino acid side chain in regiospecific oxidation of heme by heme oxygenase
    • Zhou, H., Migita, C. T., Sato, M., Sun, D. Y., Zhang, X. H., Ikeda-Saito, M., Fujii, H., and Yoshida, T. (2000) Participation of carboxylate amino acid side chain in regiospecific oxidation of heme by heme oxygenase, J. Am. Chem. Soc. 122, 8311-8312.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8311-8312
    • Zhou, H.1    Migita, C.T.2    Sato, M.3    Sun, D.Y.4    Zhang, X.H.5    Ikeda-Saito, M.6    Fujii, H.7    Yoshida, T.8
  • 34
    • 10244247769 scopus 로고    scopus 로고
    • Oxidation of the meso-methylmesoheme regioisomers by heme oxygenase
    • Torpey, J., and Ortiz de Montellano, P. R. (1996) Oxidation of the meso-methylmesoheme regioisomers by heme oxygenase, J. Biol. Chem. 271, 26067-26073.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26067-26073
    • Torpey, J.1    Ortiz De Montellano, P.R.2
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 41
    • 4243384884 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kieldgaard, M. (1991) Improved methods for binding protein models in electron density maps and the location of errors in these models, Acta Crystallogr. D54, 1017-1019.
    • (1991) Acta Crystallogr. D , vol.54 , pp. 1017-1019
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kieldgaard, M.4
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystalogr. 26, 283-291.
    • (1993) J. Appl. Crystalogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 44
    • 0028958953 scopus 로고
    • Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution
    • Wagner, U. G., Muller, N., Schmitzberger, W., Falk, H., and Kratky, C. (1995) Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution, J. Mol. Biol. 247, 326-337.
    • (1995) J. Mol. Biol. , vol.247 , pp. 326-337
    • Wagner, U.G.1    Muller, N.2    Schmitzberger, W.3    Falk, H.4    Kratky, C.5
  • 46
    • 37049108250 scopus 로고
    • Crystal and molecular structure of biliverdin dimethyl ester
    • Sheldrick, W. S. (1976) Crystal and molecular structure of biliverdin dimethyl ester, J. Chem. Soc., Perkin Trans. 2, 1457-1462.
    • (1976) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1457-1462
    • Sheldrick, W.S.1
  • 47
    • 0037732736 scopus 로고    scopus 로고
    • Steroselectivity of each of the three steps of the heme oxygenase reaction: Hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin
    • Zhang, X., Fujii, H., Matera, M., Migita, C. T., Sun, D., Sato, M., Ikeda-Saito, M., and Yoshida, T. (2003) Steroselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin, Biochemistry 42, 7418-7426.
    • (2003) Biochemistry , vol.42 , pp. 7418-7426
    • Zhang, X.1    Fujii, H.2    Matera, M.3    Migita, C.T.4    Sun, D.5    Sato, M.6    Ikeda-Saito, M.7    Yoshida, T.8
  • 48
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Liu, Y., and Ortiz de Montellano, P. R. (2000) Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1, J. Biol. Chem. 275, 5297-5307.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortiz De Montellano, P.R.2
  • 49
    • 0038165531 scopus 로고    scopus 로고
    • The binding sites of human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase
    • Wang, J., and Ortiz de Montellano, P. R. (2003) The binding sites of human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase, J. Biol. Chem 278, 20069-20076.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20069-20076
    • Wang, J.1    Ortiz De Montellano, P.R.2
  • 50
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 51
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D-photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D-photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.