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Volumn 338, Issue 1, 2005, Pages 584-589

Evidence for the hydrophobic cavity of heme oxygenase-1 to be a CO-trapping site

Author keywords

CO inhibition; CO trapping site; Heme degradation; Heme oxygenase; Kinetics; Verdoheme conversion

Indexed keywords

2 PROPANOL; CARBON MONOXIDE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; HEME OXYGENASE 1; HEMOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; VERDOHEME;

EID: 27544506562     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.045     Document Type: Article
Times cited : (4)

References (29)
  • 1
    • 0014348401 scopus 로고
    • The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase
    • R. Tenhunen, H.S. Marver, and R. Schmid The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase Proc. Natl. Acad. Sci. USA 61 1968 748 755
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 748-755
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 0020353758 scopus 로고
    • The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • T. Yoshida, M. Noguchi, and G. Kikuchi The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system J. Biol. Chem. 257 1982 9345 9348
    • (1982) J. Biol. Chem. , vol.257 , pp. 9345-9348
    • Yoshida, T.1    Noguchi, M.2    Kikuchi, G.3
  • 3
    • 0029125083 scopus 로고
    • Contributions of NO synthase and heme oxygenase to cGMP formation by cytokine and hemin-treated brain capillary endothelial cells
    • P. Vigne, E. Feolde, A. Ladoux, D. Duval, and C. Frelin Contributions of NO synthase and heme oxygenase to cGMP formation by cytokine and hemin-treated brain capillary endothelial cells Biochem. Biophys. Res. Commun. 214 1995 1 5
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 1-5
    • Vigne, P.1    Feolde, E.2    Ladoux, A.3    Duval, D.4    Frelin, C.5
  • 4
    • 0034652357 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: Evidence from genomic deletion of biosynthetic enzymes
    • L. Xue, G. Farrugia, S.M. Miller, C.D. Ferris, S.H. Snyder, and J.H. Szurszewski Carbon monoxide and nitric oxide as coneurotransmitters in the enteric nervous system: evidence from genomic deletion of biosynthetic enzymes Proc. Natl. Acad. Sci. USA 97 2000 1851 1855
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1851-1855
    • Xue, L.1    Farrugia, G.2    Miller, S.M.3    Ferris, C.D.4    Snyder, S.H.5    Szurszewski, J.H.6
  • 7
    • 0035949667 scopus 로고    scopus 로고
    • Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
    • D.E. Barañano, and S.H. Snyder Neural roles for heme oxygenase: contrasts to nitric oxide synthase Proc. Natl. Acad. Sci. USA 98 2001 10996 11002
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10996-11002
    • Barañano, D.E.1    Snyder, S.H.2
  • 8
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae
    • A. Wilks, and M.P. Schmitt Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae J. Biol. Chem. 273 1998 837 841
    • (1998) J. Biol. Chem. , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 9
    • 0034461244 scopus 로고    scopus 로고
    • Degradation of heme in Gram-negative bacteria: The product of the hem O gene of Neisseriae is a heme oxygenase
    • W. Zhu, A. Wilks, and I. Stojiljkovic Degradation of heme in Gram-negative bacteria: the product of the hem O gene of Neisseriae is a heme oxygenase J. Bacteriol. 182 2000 6783 6790
    • (2000) J. Bacteriol. , vol.182 , pp. 6783-6790
    • Zhu, W.1    Wilks, A.2    Stojiljkovic, I.3
  • 10
    • 0036914929 scopus 로고    scopus 로고
    • Expression and biochemical properties of a ferredoxin-dependent heme oxygenase required for phytochrome chromophore synthesis
    • T. Muramoto, N. Tsurui, M.J. Terry, A. Yokota, and T. Kohchi Expression and biochemical properties of a ferredoxin-dependent heme oxygenase required for phytochrome chromophore synthesis Plant Physiol. 130 2002 1958 1966
    • (2002) Plant Physiol. , vol.130 , pp. 1958-1966
    • Muramoto, T.1    Tsurui, N.2    Terry, M.J.3    Yokota, A.4    Kohchi, T.5
  • 11
    • 0037294701 scopus 로고    scopus 로고
    • Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis: Properties of the heme complex of recombinant active enzyme
    • C.T. Migita, X. Zhang, and T. Yoshida Expression and characterization of cyanobacterium heme oxygenase, a key enzyme in the phycobilin synthesis: properties of the heme complex of recombinant active enzyme Eur. J. Biochem. 270 2003 687 698
    • (2003) Eur. J. Biochem. , vol.270 , pp. 687-698
    • Migita, C.T.1    Zhang, X.2    Yoshida, T.3
  • 12
    • 2342455790 scopus 로고    scopus 로고
    • Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied
    • X. Zhang, M. Sato, M. Sasahara, C.T. Migita, and T. Yoshida Unique features of recombinant heme oxygenase of Drosophila melanogaster compared with those of other heme oxygenases studied Eur. J. Biochem. 271 2004 1713 1714
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1713-1714
    • Zhang, X.1    Sato, M.2    Sasahara, M.3    Migita, C.T.4    Yoshida, T.5
  • 13
    • 14044256465 scopus 로고    scopus 로고
    • Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase-properties of the heme and enzyme complex
    • X. Zhang, C.T. Migita, M. Sato, M. Sasahara, and T. Yoshida Protein expressed by the ho2 gene of the cyanobacterium Synechocystis sp. PCC 6803 is a true heme oxygenase-properties of the heme and enzyme complex FEBS J. 272 2005 1012 1022
    • (2005) FEBS J. , vol.272 , pp. 1012-1022
    • Zhang, X.1    Migita, C.T.2    Sato, M.3    Sasahara, M.4    Yoshida, T.5
  • 14
    • 0033732757 scopus 로고    scopus 로고
    • Mechanism of heme degradation by heme oxygenase
    • T. Yoshida, and C.T. Migita Mechanism of heme degradation by heme oxygenase J. Inorg. Biochem. 82 2000 33 41
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 33-41
    • Yoshida, T.1    Migita, C.T.2
  • 15
    • 0037898944 scopus 로고    scopus 로고
    • Autocatalytic radical reactions in physiological prosthetic heme modification
    • C. Colas, and P.R. Ortiz de Montellano Autocatalytic radical reactions in physiological prosthetic heme modification Chem. Rev. 103 2003 2305 2332
    • (2003) Chem. Rev. , vol.103 , pp. 2305-2332
    • Colas, C.1    Ortiz De Montellano, P.R.2
  • 16
    • 0017850764 scopus 로고
    • Purification and properties of heme oxygenase from pig spleen microsomes
    • T. Yoshida, and G. Kikuchi Purification and properties of heme oxygenase from pig spleen microsomes J. Biol. Chem. 253 1978 4224 4229
    • (1978) J. Biol. Chem. , vol.253 , pp. 4224-4229
    • Yoshida, T.1    Kikuchi, G.2
  • 17
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • T. Yoshida, and G. Kikuchi Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system J. Biol. Chem. 253 1978 4230 4236
    • (1978) J. Biol. Chem. , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 18
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • B.A. Schacter, E.B. Nelson, H.S. Marver, and B.S.S. Masters Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system J. Biol. Chem. 253 1972 3601 3607
    • (1972) J. Biol. Chem. , vol.253 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.S.4
  • 19
    • 0037181030 scopus 로고    scopus 로고
    • Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutant
    • R. Davydov, U. Fofman, H. Fujii, T. Yoshida, M. Ikeda-Saito, and B.M. Hoffman Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutant J. Am. Chem. Soc. 124 2002 1798 1808
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1798-1808
    • Davydov, R.1    Fofman, U.2    Fujii, H.3    Yoshida, T.4    Ikeda-Saito, M.5    Hoffman, B.M.6
  • 21
    • 0032127571 scopus 로고    scopus 로고
    • Phytobilin biosynthesis:cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803
    • J. Cornejo, R.D. Willows, and S.I. Beale Phytobilin biosynthesis:cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803 Plant J. 15 1998 99 107
    • (1998) Plant J. , vol.15 , pp. 99-107
    • Cornejo, J.1    Willows, R.D.2    Beale, S.I.3
  • 23
    • 4143105792 scopus 로고    scopus 로고
    • CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: Mechanism of escaping from product inhibition
    • M. Sugishima, H. Sakamoto, M. Noguchi, and K. Fukuyama CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: mechanism of escaping from product inhibition J. Mol. Biol. 341 2004 7 13
    • (2004) J. Mol. Biol. , vol.341 , pp. 7-13
    • Sugishima, M.1    Sakamoto, H.2    Noguchi, M.3    Fukuyama, K.4
  • 24
    • 9644264176 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme
    • M. Sugishima, C.T. Migita, X. Zhang, T. Yoshida, and K. Fukuyama Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme Eur. J. Biochem. 271 2004 4517 4525
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4517-4525
    • Sugishima, M.1    Migita, C.T.2    Zhang, X.3    Yoshida, T.4    Fukuyama, K.5
  • 25
    • 0024397098 scopus 로고
    • Human NADPH-P450 oxidoreductase: Complementary DNA cloning, sequence and vaccina virus-mediated expression and localization of the CYPOR gene to chromosome 7
    • S. Yamano, O.W. McBride, J.P. Hardwick, H.V. Gelboin, and F.J. Gonzalez Human NADPH-P450 oxidoreductase: complementary DNA cloning, sequence and vaccina virus-mediated expression and localization of the CYPOR gene to chromosome 7 Mol. Pharmacol. 36 1989 83 88
    • (1989) Mol. Pharmacol. , vol.36 , pp. 83-88
    • Yamano, S.1    McBride, O.W.2    Hardwick, J.P.3    Gelboin, H.V.4    Gonzalez, F.J.5
  • 27
    • 0001454446 scopus 로고
    • Expression of maize ferredoxin cDNA in Escherichia coli
    • T. Hase, S. Mizutani, and Y. Mukohata Expression of maize ferredoxin cDNA in Escherichia coli Plant Physiol. 97 1991 1395 1401
    • (1991) Plant Physiol. , vol.97 , pp. 1395-1401
    • Hase, T.1    Mizutani, S.2    Mukohata, Y.3
  • 29
    • 0040141555 scopus 로고    scopus 로고
    • Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
    • Y. Liu, and P.O. OrtizdeMotellano Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1 J. Biol. Chem. 275 2000 5297 5307
    • (2000) J. Biol. Chem. , vol.275 , pp. 5297-5307
    • Liu, Y.1    Ortizdemotellano, P.O.2


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