메뉴 건너뛰기




Volumn 269, Issue 21, 2002, Pages 5231-5239

The reactivity of α-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite

Author keywords

hydroxyhaem; Haem oxygenase; NADPH cytochrome P450 reductase; Sodium dithionite; Verdohaem

Indexed keywords

ALPHA HYDROXYHAEM; BILIVERDIN; HEME DERIVATIVE; HEME OXYGENASE 1; IRON DERIVATIVE; OXYGEN; SODIUM DITHIONITE; UNCLASSIFIED DRUG; VERDOHAEM;

EID: 0036428431     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03230.x     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 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
  • 2
    • 0033973712 scopus 로고    scopus 로고
    • The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties
    • Ryter, S.W. & Tyrrell, R.M. (2000) The heme synthesis and degradation pathways: Role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties. Free Radic. Biol. Med. 28, 289-309.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 289-309
    • Ryter, S.W.1    Tyrrell, R.M.2
  • 4
    • 0032757252 scopus 로고    scopus 로고
    • The heme oxygenase pathway and its interaction with nitric oxide in the control of cellular homeostasis
    • Foresti, R. & Motterlini, R. (1999) The heme oxygenase pathway and its interaction with nitric oxide in the control of cellular homeostasis. Free Radic. Res. 31, 459-475.
    • (1999) Free Radic. Res. , vol.31 , pp. 459-475
    • Foresti, R.1    Motterlini, R.2
  • 5
  • 6
    • 0035012930 scopus 로고    scopus 로고
    • The case of CO signaling: Why the jury is still out
    • Cary, S.P.L. & Marletta, M.A. (2001) The case of CO signaling: Why the jury is still out. J. Clin. Invest. 107, 1071-1073.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1071-1073
    • Cary, S.P.L.1    Marletta, M.A.2
  • 7
    • 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. & 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
  • 9
    • 0019590350 scopus 로고
    • Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: Involvement of hydroxyheme in the sequence of heme catabolism
    • Yoshida, T., Noguchi, M., Kikuchi, G. & Sano, S. (1981) Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: Involvement of hydroxyheme in the sequence of heme catabolism. J. Biochem. (Tokyo) 90, 125-131
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 125-131
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3    Sano, S.4
  • 12
    • 0020742627 scopus 로고
    • A stoichiometric study of heme degradation catalyzed by the reconstituted heme oxygenase system with special consideration of the production of hydrogen peroxide during the reaction
    • Noguchi, M., Yoshida, T. & Kikuchi, G. (1983) A stoichiometric study of heme degradation catalyzed by the reconstituted heme oxygenase system with special consideration of the production of hydrogen peroxide during the reaction. J. Biochem. (Tokyo) 93, 1027-1036.
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 1027-1036
    • Noguchi, M.1    Yoshida, T.2    Kikuchi, G.3
  • 13
    • 0027440198 scopus 로고
    • Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species
    • Wilks, A. & Ortiz de Montellano, P.R. (1993) Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species. J. Biol. Chem. 268, 22357-22362.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22357-22362
    • Wilks, A.1    Ortiz de Montellano, P.R.2
  • 14
    • 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. & 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
  • 15
    • 35448942011 scopus 로고    scopus 로고
    • Heme oxygenase structure and mechanism
    • Sykes, A.G., ed. Academic Press, San Diego
    • Ortiz de Montellano, P.R. & Wilks, A. (2001) Heme oxygenase structure and mechanism. In Advances in Inorganic Chemistry, Vol. 51 (Sykes, A.G., ed.), pp. 359-407. Academic Press, San Diego.
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 359-407
    • Ortiz de Montellano, P.R.1    Wilks, A.2
  • 16
    • 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. & Hooman, 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    Hooman, B.M.4
  • 18
    • 0000958371 scopus 로고
    • Electronic states of iron oxyporphyrin and verdohemochrome obtained by coupled oxidation of iron porphyrin
    • Sano, S., Sugiura, Y., Maeda, Y., Ogawa, S. & Morishima, I. (1981) Electronic states of iron oxyporphyrin and verdohemochrome obtained by coupled oxidation of iron porphyrin. J. Am. Chem. Soc. 103, 2888-2890.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 2888-2890
    • Sano, S.1    Sugiura, Y.2    Maeda, Y.3    Ogawa, S.4    Morishima, I.5
  • 19
    • 0001624954 scopus 로고
    • NMR studies of metalloporphyrin radicals. Iron (II) oxohplorin radical formed from iron (III) meso-hydroxyoctaethylporphyrin
    • Morishima, I., Fujii, H., Shiro, Y. & Sano, S. (1986) NMR studies of metalloporphyrin radicals. Iron (II) oxohplorin radical formed from iron (III) meso-hydroxyoctaethylporphyrin. J. Am. Chem. Soc. 108, 3858-3860.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 3858-3860
    • Morishima, I.1    Fujii, H.2    Shiro, Y.3    Sano, S.4
  • 20
    • 0023657743 scopus 로고
    • Radical intermediates in the oxidation of octaethylheme to octaethylverdoheme
    • Masuoka, N. & Itano, H.A. (1987) Radical intermediates in the oxidation of octaethylheme to octaethylverdoheme. Biochemistry 26, 3672-3680.
    • (1987) Biochemistry , vol.26 , pp. 3672-3680
    • Masuoka, N.1    Itano, H.A.2
  • 21
    • 0000419118 scopus 로고
    • Studies on the iron (II) meso-oxyporphyrin π-neutral radical as a reaction intermediate in heme catabolism
    • Morishima, I., Fujii, H., Shiro, Y. & Sano, S. (1995) Studies on the iron (II) meso-oxyporphyrin π-neutral radical as a reaction intermediate in heme catabolism. Inorg. Chem. 34, 1528-1535.
    • (1995) Inorg. Chem. , vol.34 , pp. 1528-1535
    • Morishima, I.1    Fujii, H.2    Shiro, Y.3    Sano, S.4
  • 22
    • 0022668643 scopus 로고
    • On the mechanism of the chemical and enzymic oxgenations of α-oxyprotohemin IX to Fe·biliverdin IXα
    • Sano, S., Sano, T., Morishima, I., Shiro, Y. & Maeda, Y. (1986) On the mechanism of the chemical and enzymic oxgenations of α-oxyprotohemin IX to Fe·biliverdin IXα. Proc. Natl Acad. Sci. USA 83, 531-535.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 531-535
    • Sano, S.1    Sano, T.2    Morishima, I.3    Shiro, Y.4    Maeda, Y.5
  • 23
    • 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. & 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
  • 24
    • 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. & 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
  • 25
    • 0033797523 scopus 로고    scopus 로고
    • Coordination chemistry with meso-hydroxylated porphyrins (oxophlorins), intermediates in heme degradation
    • Balch, A.L. (2000) Coordination chemistry with meso-hydroxylated porphyrins (oxophlorins), intermediates in heme degradation. Coord. Chem. Rev. 200-202, 349-377.
    • (2000) Coord. Chem. Rev. , vol.200-202 , pp. 349-377
    • Balch, A.L.1
  • 27
    • 0009611092 scopus 로고    scopus 로고
    • Molecular oxygen oxidizes the porphyrin ring of the ferric α-hydroxyheme in heme oxygenase in the absence of reducing equivalent
    • Migita, C.T., Fujii, H., Matera, K.M., Takahashi, S., Zhou, H. & Yoshida, T. (1999) Molecular oxygen oxidizes the porphyrin ring of the ferric α-hydroxyheme in heme oxygenase in the absence of reducing equivalent. 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
  • 29
    • 0032169653 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme
    • Omata, Y., Asada, S., Sakamoto, H., Fukuyama, K. & Noguchi, M. (1998) Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme. Acta Crystallogr. D54, 1017-1019.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 1017-1019
    • Omata, Y.1    Asada, S.2    Sakamoto, H.3    Fukuyama, K.4    Noguchi, M.5
  • 30
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y. & Masters, B.S.B. (1976) Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251, 5337-5344.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.B.2
  • 31
    • 0033733182 scopus 로고    scopus 로고
    • Separation and identification of the regioisomers of verdoheme by reversed-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase
    • Sakamoto, H., Omata, Y., Adachi, Y., Palmer, G. & Noguchi, M. (2000) Separation and identification of the regioisomers of verdoheme by reversed-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase. J. Inorg. Biochem. 82, 113-121.
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 113-121
    • Sakamoto, H.1    Omata, Y.2    Adachi, Y.3    Palmer, G.4    Noguchi, M.5
  • 32
    • 0014478112 scopus 로고
    • A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution
    • Burleigh Jr, B.D., Foust, G.P. & Williams, S. (1969) A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution. Anal. Biochem. 27, 536-544.
    • (1969) Anal. Biochem. , vol.27 , pp. 536-544
    • Burleigh B.D., Jr.1    Foust, G.P.2    Williams, S.3
  • 33
    • 0017567414 scopus 로고
    • A versatile apparatus for performing anaerobic optical titrations with provision for mutiple sampling of the reaction mixture
    • Palmer, G. (1977) A versatile apparatus for performing anaerobic optical titrations with provision for mutiple sampling of the reaction mixture. Anal. Biochem. 83, 597-608.
    • (1977) Anal. Biochem. , vol.83 , pp. 597-608
    • Palmer, G.1
  • 36
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • Yoshida, T. & Kikuchi, G. (1978) Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 253, 4230-4236.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 38
    • 37049077217 scopus 로고
    • Detection of octaethylverdohaem π-neutral radical by electrochemical-optical absorption and -ESR measurements
    • Tajima, K., Tada, K., Yasui, A., Ohya-Nishiguchi, H. & Ishizu, K. (1993) Detection of octaethylverdohaem π-neutral radical by electrochemical-optical absorption and -ESR measurements. J. Chem. Soc. Chem. Commun. 282-284.
    • (1993) J. Chem. Soc. Chem. Commun. , pp. 282-284
    • Tajima, K.1    Tada, K.2    Yasui, A.3    Ohya-Nishiguchi, H.4    Ishizu, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.