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Volumn 23, Issue 3, 2009, Pages 379-387

Comparison of the crystal structure and function to wild-type and His25Ala mutant human heme oxygenase-1

Author keywords

Activity; Crystal structure; Human heme oxygenase 1; Mutant

Indexed keywords

ALANINE; HEME OXYGENASE 1; HISTONE; HEME; HMOX1 PROTEIN, HUMAN; IRON;

EID: 64249100287     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm_00000142     Document Type: Article
Times cited : (4)

References (49)
  • 1
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen R, Marver HS and Schmid R: Microsomal heme oxygenase. Characterization of the enzyme. J Biol Chem 244: 6388-6394, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 2
    • 0018693560 scopus 로고
    • Induction of hepatic heme oxygenase activity by bromobenzene
    • Guzelian PS and Elshourbagy NA: Induction of hepatic heme oxygenase activity by bromobenzene. Arch Biochem Biophys 196: 178-185, 1979.
    • (1979) Arch Biochem Biophys , vol.196 , pp. 178-185
    • Guzelian, P.S.1    Elshourbagy, N.A.2
  • 3
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: A regulator of second messenger gases
    • Maines MD: The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol 37: 517-554, 1997.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 4
    • 0031214204 scopus 로고    scopus 로고
    • New physiological importance of two classic residual products: Carbon monoxide and bilirubin
    • Marilena G: New physiological importance of two classic residual products: carbon monoxide and bilirubin. Biochem Mol Med 61: 136-142, 1997.
    • (1997) Biochem Mol Med , vol.61 , pp. 136-142
    • Marilena, G.1
  • 5
    • 0036073379 scopus 로고    scopus 로고
    • Rickettsia rickettsii infection of cultured human endothelial cells induces heme oxygenase 1 expression
    • Rydkina E, Sahni A, Silverman DJ and Sahni SK: Rickettsia rickettsii infection of cultured human endothelial cells induces heme oxygenase 1 expression. Infect Immun 70: 4045-4052, 2002.
    • (2002) Infect Immun , vol.70 , pp. 4045-4052
    • Rydkina, E.1    Sahni, A.2    Silverman, D.J.3    Sahni, S.K.4
  • 6
    • 0035012930 scopus 로고    scopus 로고
    • The case of CO signaling: Why the jury is still out
    • Cary SP and Marletta MA: The case of CO signaling: why the jury is still out. J Clin Invest 107: 1071-1073, 2001.
    • (2001) J Clin Invest , vol.107 , pp. 1071-1073
    • Cary, S.P.1    Marletta, M.A.2
  • 7
    • 0035865183 scopus 로고    scopus 로고
    • A functional link between heme oxygenase and cyclo-oxygenase activities in cortical rat astrocytes
    • Vairano M, Dello RC, Pozzoli G, Tringali G, Preziosi P and Navarra P: A functional link between heme oxygenase and cyclo-oxygenase activities in cortical rat astrocytes. Biochem Pharmacol 61: 437-441, 2001.
    • (2001) Biochem Pharmacol , vol.61 , pp. 437-441
    • Vairano, M.1    Dello, R.C.2    Pozzoli, G.3    Tringali, G.4    Preziosi, P.5    Navarra, P.6
  • 10
    • 0015295105 scopus 로고
    • Method for microassay of microsomal heme oxygenase activity
    • Tenhunen R: Method for microassay of microsomal heme oxygenase activity. Anal Biochem 45: 600-607, 1972.
    • (1972) Anal Biochem , vol.45 , pp. 600-607
    • Tenhunen, R.1
  • 11
    • 0017850764 scopus 로고
    • Purification and properties of heme oxygenase from pig spleen microsomes
    • Yoshida T and Kikuchi G: Purification and properties of heme oxygenase from pig spleen microsomes. J Biol Chem 253: 4224-4229, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 4224-4229
    • Yoshida, T.1    Kikuchi, G.2
  • 12
    • 0018786841 scopus 로고
    • Purification and properties of heme oxygenase from rat liver microsomes
    • Yoshida T and Kikuchi G: Purification and properties of heme oxygenase from rat liver microsomes. J Biol Chem 254: 4487-4491, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 4487-4491
    • Yoshida, T.1    Kikuchi, G.2
  • 13
    • 0016613065 scopus 로고
    • Sequence of heme decomposition by the coupled oxidation of myoglobin with ascorbic acid
    • Yoshida T and Kikuchi G: Sequence of heme decomposition by the coupled oxidation of myoglobin with ascorbic acid. Tohoku J Exp Med 115: 67-74, 1975.
    • (1975) Tohoku J Exp Med , vol.115 , pp. 67-74
    • Yoshida, T.1    Kikuchi, G.2
  • 15
    • 0023654799 scopus 로고
    • Nucleotide sequence and organization of the rat heme oxygenase gene
    • Muller RM, Taguchi H and Shibahara S: Nucleotide sequence and organization of the rat heme oxygenase gene. J Biol Chem 262: 6795-6802, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 6795-6802
    • Muller, R.M.1    Taguchi, H.2    Shibahara, S.3
  • 16
    • 24644517828 scopus 로고    scopus 로고
    • Heme oxygenase-1: From bench to bedside
    • Morse D and Choi AM: Heme oxygenase-1: from bench to bedside. Am J Respir Crit Care Med 172: 660-670, 2005.
    • (2005) Am J Respir Crit Care Med , vol.172 , pp. 660-670
    • Morse, D.1    Choi, A.M.2
  • 17
    • 19544370917 scopus 로고    scopus 로고
    • Heme oxygenase and the cardiovascular-renal system
    • Abraham NG and Kappas A: Heme oxygenase and the cardiovascular-renal system. Free Radic Biol Med 39: 1-25, 2005.
    • (2005) Free Radic Biol Med , vol.39 , pp. 1-25
    • Abraham, N.G.1    Kappas, A.2
  • 20
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss KD and Tonegawa S: Reduced stress defense in heme oxygenase 1-deficient cells. Proc Natl Acad Sci USA 94: 10925-10930, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 22
    • 0035707492 scopus 로고    scopus 로고
    • Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs
    • Soares MP, Brouard S, Smith RN and Bach FH: Heme oxygenase-1, a protective gene that prevents the rejection of transplanted organs. Immunol Rev 184: 275-285, 2001.
    • (2001) Immunol Rev , vol.184 , pp. 275-285
    • Soares, M.P.1    Brouard, S.2    Smith, R.N.3    Bach, F.H.4
  • 23
    • 0042838097 scopus 로고    scopus 로고
    • Graft protective effects of heme oxygenase 1 in mouse tracheal transplant-related obliterative bronchiolitis
    • Visner GA, Lu F, Zhou H, Latham C, Agarwal A and Zander DS: Graft protective effects of heme oxygenase 1 in mouse tracheal transplant-related obliterative bronchiolitis. Transplantation 76: 650-656, 2003.
    • (2003) Transplantation , vol.76 , pp. 650-656
    • Visner, G.A.1    Lu, F.2    Zhou, H.3    Latham, C.4    Agarwal, A.5    Zander, D.S.6
  • 24
    • 0008881566 scopus 로고    scopus 로고
    • The heme oxygenase system and its functions in the brain
    • Maines MD: The heme oxygenase system and its functions in the brain. Cell Mol Biol 46: 573-585, 2000.
    • (2000) Cell Mol Biol , vol.46 , pp. 573-585
    • Maines, M.D.1
  • 25
    • 0027985134 scopus 로고
    • Identification of histidine 25 as the heme ligand in human liver heme oxygenase
    • Sun J, Loehr TM, Wilks A and Ortiz de Montellano PR: Identification of histidine 25 as the heme ligand in human liver heme oxygenase. Biochemistry 33: 13734-13740, 1994.
    • (1994) Biochemistry , vol.33 , pp. 13734-13740
    • Sun, J.1    Loehr, T.M.2    Wilks, A.3    Ortiz de Montellano, P.R.4
  • 28
    • 0035323272 scopus 로고    scopus 로고
    • The preparation of rat heme oxygenase-1 mutant to reduce the level of bilirubin
    • Xia ZW, Shao J, Shen QX, Wang J, Li YZ, Chen S, Yu SC. The preparation of rat heme oxygenase-1 mutant to reduce the level of bilirubin. Chin Med J 114: 348-351, 2001.
    • (2001) Chin Med J , vol.114 , pp. 348-351
    • Xia, Z.W.1    Shao, J.2    Shen, Q.X.3    Wang, J.4    Li, Y.Z.5    Chen, S.6    Yu, S.C.7
  • 30
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath JW: The finer things in X-ray diffraction data collection. Acta Crystallogr D Biol Crystallogr 55: 1718-1725, 1999.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW and Kjeldgaard M: Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119, 1991.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 64849107288 scopus 로고    scopus 로고
    • Delano Scientific LLC. San Carlos
    • Delano W: The PyMol Molecular Graphics System. (http://www.pymol.org) Delano Scientific LLC. San Carlos, 2002.
    • (2002)
    • Delano, W.1
  • 35
    • 0035949642 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
    • Schuller DJ, Zhu W, Stojiljkovic I, Wilks A and Poulos T: Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1. Biochemistry 40: 11552-11558, 2001.
    • (2001) Biochemistry , vol.40 , pp. 11552-11558
    • Schuller, D.J.1    Zhu, W.2    Stojiljkovic, I.3    Wilks, A.4    Poulos, T.5
  • 36
    • 0033597730 scopus 로고    scopus 로고
    • Heme degradation as catalyzed by a recombinant bacterial heme oxygenase, (HmuO) from Corynebacterium diphtheriae
    • Chu GC, Katakura K, Zhang X, Yoshida T and Ikeda-Saito M: Heme degradation as catalyzed by a recombinant bacterial heme oxygenase, (HmuO) from Corynebacterium diphtheriae. J Biol Chem 274: 21319-21325, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 21319-21325
    • Chu, G.C.1    Katakura, K.2    Zhang, X.3    Yoshida, T.4    Ikeda-Saito, M.5
  • 37
    • 0035834012 scopus 로고    scopus 로고
    • Regulation of human heme oxygenase in endothelial cells by using sense and antisense retroviral constructs
    • Quan S, Yang L, Abraham NG and Kappas A: Regulation of human heme oxygenase in endothelial cells by using sense and antisense retroviral constructs. Proc Natl Acad Sci USA 98: 12203-12208, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12203-12208
    • Quan, S.1    Yang, L.2    Abraham, N.G.3    Kappas, A.4
  • 38
    • 0037127305 scopus 로고    scopus 로고
    • Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response
    • Chang SH, Barbosa TI, Chen C, Kilberg MS and Agarwal A: Glucose deprivation induces heme oxygenase-1 gene expression by a pathway independent of the unfolded protein response. J Biol Chem 277: 1933-1940, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 1933-1940
    • Chang, S.H.1    Barbosa, T.I.2    Chen, C.3    Kilberg, M.S.4    Agarwal, A.5
  • 39
    • 0039488237 scopus 로고    scopus 로고
    • Zhang M, An W and Du HJ: Increased resistance against oxidant-induced injury in the rat vascular smooth muscle cells transfected with human heme oxygenase-1 gene. Sheng Li Xue Bao 54: 12-16, 2002.
    • Zhang M, An W and Du HJ: Increased resistance against oxidant-induced injury in the rat vascular smooth muscle cells transfected with human heme oxygenase-1 gene. Sheng Li Xue Bao 54: 12-16, 2002.
  • 41
    • 0026529972 scopus 로고
    • Importance of histidine residue 25 of rat heme oxygenase for its catalytic activity
    • Ishikawa K, Sato M, Ito M and Yoshida T: Importance of histidine residue 25 of rat heme oxygenase for its catalytic activity. Biochem Biophys Res Commun 182: 981-986, 1992.
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 981-986
    • Ishikawa, K.1    Sato, M.2    Ito, M.3    Yoshida, T.4
  • 42
    • 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 SM, Miller WL and Ortiz de Montellano PR: 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.
    • (1995) Biochemistry , vol.34 , pp. 4421-4427
    • Wilks, A.1    Black, S.M.2    Miller, W.L.3    Ortiz de Montellano, P.R.4
  • 43
    • 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 PR and Poulos TL: 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.
    • (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
  • 45
    • 17644366432 scopus 로고    scopus 로고
    • Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity
    • Lad L, Koshkin A, Ortiz de Montellano PR and Poulos TL: Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity. J Biol Inorg Chem 10: 138-146, 2005.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 138-146
    • Lad, L.1    Koshkin, A.2    Ortiz de Montellano, P.R.3    Poulos, T.L.4
  • 47
    • 39049139022 scopus 로고    scopus 로고
    • Quantum mechanical/molecular mechanical study of mechanisms of heme degradation by the enzyme heme oxygenase: The strategic function of the water cluster
    • Chen H, Moreau Y, Derat E and Shaik S: Quantum mechanical/molecular mechanical study of mechanisms of heme degradation by the enzyme heme oxygenase: the strategic function of the water cluster. J Am Chem Soc 130: 1953-1965, 2008.
    • (2008) J Am Chem Soc , vol.130 , pp. 1953-1965
    • Chen, H.1    Moreau, Y.2    Derat, E.3    Shaik, S.4
  • 48
    • 0028909671 scopus 로고
    • Demonstration that histidine-25, but not histidine-132, is the axial heme ligand in rat heme oxygenase-1
    • Itomaki M, Ishikawa K, Matera KM, Sato M, Ikedasaito M and Yoshida T: Demonstration that histidine-25, but not histidine-132, is the axial heme ligand in rat heme oxygenase-1. Arch Biochem Biophys 317: 253-258, 1995.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 253-258
    • Itomaki, M.1    Ishikawa, K.2    Matera, K.M.3    Sato, M.4    Ikedasaito, M.5    Yoshida, T.6


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