메뉴 건너뛰기




Volumn 48, Issue 11, 2010, Pages 1548-1558

Nitric oxide blocks cellular heme insertion into a broad range of heme proteins

Author keywords

Cytochrome P450; Free radicals; Gene expression; Heat shock protein; Heme; Hemoglobin

Indexed keywords

3,3 BIS(2 AMINOETHYL) 1 HYDROXY 2 OXOTRIAZENE; ADENOSINE TRIPHOSPHATE; APOPROTEIN; CATALASE; CYTOCHROME P450; GUANYLATE CYCLASE; HEME; HEMOGLOBIN; HEMOPROTEIN; NITRIC OXIDE; NITRIC OXIDE DONOR; NITRIC OXIDE SYNTHASE; PROTOPORPHYRIN;

EID: 77952553811     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.02.038     Document Type: Article
Times cited : (48)

References (106)
  • 1
    • 34249823650 scopus 로고    scopus 로고
    • The chemistry and biochemistry of heme proteins
    • Raven E., Ortiz de Montellano P.R. The chemistry and biochemistry of heme proteins. Nat. Prod. Rep. 2007, 24:499.
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 499
    • Raven, E.1    Ortiz de Montellano, P.R.2
  • 2
    • 0036260085 scopus 로고    scopus 로고
    • Structure-function relationships in heme-proteins
    • Paoli M., Marles-Wright J., Smith A. Structure-function relationships in heme-proteins. DNA Cell Biol. 2002, 21:271-280.
    • (2002) DNA Cell Biol. , vol.21 , pp. 271-280
    • Paoli, M.1    Marles-Wright, J.2    Smith, A.3
  • 4
    • 27544481297 scopus 로고    scopus 로고
    • Structural biology of heme monooxygenases
    • Poulos T.L. Structural biology of heme monooxygenases. Biochem. Biophys. Res. Commun. 2005, 338:337-345.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 337-345
    • Poulos, T.L.1
  • 5
    • 39749108827 scopus 로고    scopus 로고
    • Revisiting heme mechanisms: a perspective on the mechanisms of nitric oxide synthase (NOS), heme oxygenase (HO), and cytochrome P450s (CYP450s)
    • Zhu Y., Silverman R.B. Revisiting heme mechanisms: a perspective on the mechanisms of nitric oxide synthase (NOS), heme oxygenase (HO), and cytochrome P450s (CYP450s). Biochemistry 2008, 47:2231-2243.
    • (2008) Biochemistry , vol.47 , pp. 2231-2243
    • Zhu, Y.1    Silverman, R.B.2
  • 6
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: from molecular mechanisms to health implications
    • Davies M.J., Hawkins C.L., Pattison D.I., Rees M.D. Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid. Redox Signal. 2008, 10:1199-1234.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 7
    • 0035313335 scopus 로고    scopus 로고
    • Recent advances in heme-protein sensors
    • Chan M.K. Recent advances in heme-protein sensors. Curr. Opin. Chem. Biol. 2001, 5:216-222.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 216-222
    • Chan, M.K.1
  • 9
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka P. Cell biology of heme. Am. J. Med. Sci. 1999, 318:241-256.
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 10
    • 34249821051 scopus 로고    scopus 로고
    • The Janus nature of heme
    • Poulos T.L. The Janus nature of heme. Nat. Prod. Rep. 2007, 24:504-510.
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 504-510
    • Poulos, T.L.1
  • 12
    • 54049093319 scopus 로고    scopus 로고
    • Mechanisms of heme iron absorption: current questions and controversies
    • West A.R., Oates P.S. Mechanisms of heme iron absorption: current questions and controversies. World J. Gastroenterol. 2008, 14:4101-4110.
    • (2008) World J. Gastroenterol. , vol.14 , pp. 4101-4110
    • West, A.R.1    Oates, P.S.2
  • 13
    • 68949122857 scopus 로고    scopus 로고
    • Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state
    • Yi L., Jenkins P.M., Leichert L.I., Jakob U., Martens J.R., Ragsdale S.W. Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. J. Biol. Chem. 2009, 284:20556-20561.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20556-20561
    • Yi, L.1    Jenkins, P.M.2    Leichert, L.I.3    Jakob, U.4    Martens, J.R.5    Ragsdale, S.W.6
  • 14
    • 33744493616 scopus 로고    scopus 로고
    • Heme as key regulator of major mammalian cellular functions: molecular, cellular, and pharmacological aspects
    • Tsiftsoglou A.S., Tsamadou A.I., Papadopoulou L.C. Heme as key regulator of major mammalian cellular functions: molecular, cellular, and pharmacological aspects. Pharmacol. Ther. 2006, 111:327-345.
    • (2006) Pharmacol. Ther. , vol.111 , pp. 327-345
    • Tsiftsoglou, A.S.1    Tsamadou, A.I.2    Papadopoulou, L.C.3
  • 16
    • 0022401009 scopus 로고
    • A protein of the Z class of liver cytosolic proteins in the rat that preferentially binds heme
    • Vincent S.H., Muller-Eberhard U. A protein of the Z class of liver cytosolic proteins in the rat that preferentially binds heme. J. Biol. Chem. 1985, 260:14521-14528.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14521-14528
    • Vincent, S.H.1    Muller-Eberhard, U.2
  • 17
    • 0020429882 scopus 로고
    • Binding of heme by glutathione S-transferase: a possible role of the erythrocyte enzyme
    • Harvey J.W., Beutler E. Binding of heme by glutathione S-transferase: a possible role of the erythrocyte enzyme. Blood 1982, 60:1227-1230.
    • (1982) Blood , vol.60 , pp. 1227-1230
    • Harvey, J.W.1    Beutler, E.2
  • 20
    • 44949200347 scopus 로고    scopus 로고
    • Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms
    • Kitanishi K., Igarashi J., Hayasaka K., Hikage N., Saiful I., Yamauchi S., Uchida T., Ishimori K., Shimizu T. Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochemistry 2008, 47:6157-6168.
    • (2008) Biochemistry , vol.47 , pp. 6157-6168
    • Kitanishi, K.1    Igarashi, J.2    Hayasaka, K.3    Hikage, N.4    Saiful, I.5    Yamauchi, S.6    Uchida, T.7    Ishimori, K.8    Shimizu, T.9
  • 21
    • 17844393421 scopus 로고    scopus 로고
    • Acquisition, mobilization and utilization of cellular iron and heme: endless findings and growing evidence of tight regulation
    • Taketani S. Acquisition, mobilization and utilization of cellular iron and heme: endless findings and growing evidence of tight regulation. Tohoku J. Exp. Med. 2005, 205:297-318.
    • (2005) Tohoku J. Exp. Med. , vol.205 , pp. 297-318
    • Taketani, S.1
  • 22
    • 85011195923 scopus 로고
    • The synthesis and turnover of rat liver peroxisomes. V. Intracellular pathway of catalase synthesis
    • Lazarow P.B., de Duve C. The synthesis and turnover of rat liver peroxisomes. V. Intracellular pathway of catalase synthesis. J. Cell Biol. 1973, 59:507-524.
    • (1973) J. Cell Biol. , vol.59 , pp. 507-524
    • Lazarow, P.B.1    de Duve, C.2
  • 23
    • 0026474687 scopus 로고
    • Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase
    • Nauseef W.M., McCormick S., Yi H. Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase. Blood 1992, 80:2622-2633.
    • (1992) Blood , vol.80 , pp. 2622-2633
    • Nauseef, W.M.1    McCormick, S.2    Yi, H.3
  • 25
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias
    • Jane-Jane C. Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias. Blood 2007, 109:2693-2699.
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Jane-Jane, C.1
  • 26
    • 0027479724 scopus 로고
    • A double life: cytosolic aconitase as a regulatory RNA binding protein
    • Klausner R.D., Rouault T.A. A double life: cytosolic aconitase as a regulatory RNA binding protein. Mol. Biol. Cell 1993, 4:1-5.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1-5
    • Klausner, R.D.1    Rouault, T.A.2
  • 27
    • 0035253023 scopus 로고    scopus 로고
    • Nitric oxide and the regulation of gene expression
    • Bogdan C. Nitric oxide and the regulation of gene expression. Trends Cell Biol. 2001, 11:66-75.
    • (2001) Trends Cell Biol. , vol.11 , pp. 66-75
    • Bogdan, C.1
  • 28
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 1997, 89:1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 29
    • 0029935269 scopus 로고    scopus 로고
    • Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability
    • Albakri Q.A., Stuehr D.J. Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability. J. Biol. Chem. 1996, 271:5414-5421.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5414-5421
    • Albakri, Q.A.1    Stuehr, D.J.2
  • 30
    • 0021358270 scopus 로고
    • Long-term cultivation and differentiation of human erythroleukemia cells in a protein-free chemically defined medium
    • Okabe T., Fujisawa M., Takaku F. Long-term cultivation and differentiation of human erythroleukemia cells in a protein-free chemically defined medium. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:453-455.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 453-455
    • Okabe, T.1    Fujisawa, M.2    Takaku, F.3
  • 31
    • 0027174021 scopus 로고
    • Protection of human endothelial cells from oxidant injury by adenovirus-mediated transfer of the human catalase cDNA
    • Erzurum S.C., Lemarchand P., Rosenfeld M.A., Yoo J.H., Crystal R.G. Protection of human endothelial cells from oxidant injury by adenovirus-mediated transfer of the human catalase cDNA. Nucleic Acids Res. 1993, 21:1607-1612.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1607-1612
    • Erzurum, S.C.1    Lemarchand, P.2    Rosenfeld, M.A.3    Yoo, J.H.4    Crystal, R.G.5
  • 32
    • 0035883891 scopus 로고    scopus 로고
    • Heterologous expression of cytochrome P450 2D6 mutants, electron transfer, and catalysis of bufuralol hydroxylation: the role of aspartate 301 in structural integrity
    • Hanna I.H., Kim M.S., Guengerich F.P. Heterologous expression of cytochrome P450 2D6 mutants, electron transfer, and catalysis of bufuralol hydroxylation: the role of aspartate 301 in structural integrity. Arch. Biochem. Biophys. 2001, 393:255-261.
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 255-261
    • Hanna, I.H.1    Kim, M.S.2    Guengerich, F.P.3
  • 33
    • 0034705191 scopus 로고    scopus 로고
    • Elucidation of distinct ligand binding sites for cytochrome P450 3A4
    • Hosea N.A., Miller G.P., Guengerich F.P. Elucidation of distinct ligand binding sites for cytochrome P450 3A4. Biochemistry 2000, 39:5929-5939.
    • (2000) Biochemistry , vol.39 , pp. 5929-5939
    • Hosea, N.A.1    Miller, G.P.2    Guengerich, F.P.3
  • 34
    • 0031416373 scopus 로고    scopus 로고
    • Substrate binding and calmodulin binding to endothelial nitric oxide synthase coregulate its enzymatic activity
    • Presta A., Liu J., Sessa W.C., Stuehr D.J. Substrate binding and calmodulin binding to endothelial nitric oxide synthase coregulate its enzymatic activity. Nitric Oxide 1997, 1:74-87.
    • (1997) Nitric Oxide , vol.1 , pp. 74-87
    • Presta, A.1    Liu, J.2    Sessa, W.C.3    Stuehr, D.J.4
  • 35
    • 0026471538 scopus 로고
    • Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide
    • McMillan K., Bredt D.S., Hirsch D.J., Snyder S.H., Clark J.E., Masters B.S. Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:11141-11145.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11141-11145
    • McMillan, K.1    Bredt, D.S.2    Hirsch, D.J.3    Snyder, S.H.4    Clark, J.E.5    Masters, B.S.6
  • 37
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric oxide synthases: cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical
    • Stuehr D.J., Ikeda-Saito M. Spectral characterization of brain and macrophage nitric oxide synthases: cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical. J. Biol. Chem. 1992, 267:20547-20550.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda-Saito, M.2
  • 38
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 1964, 239:2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 40
    • 0029929385 scopus 로고    scopus 로고
    • Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin
    • Klatt P., Pfeiffer S., List B.M., Lehner D., Glatter O., Bachinger H.P., Werner E.R., Schmidt K., Mayer B. Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin. J. Biol. Chem. 1996, 271:7336-7342.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7336-7342
    • Klatt, P.1    Pfeiffer, S.2    List, B.M.3    Lehner, D.4    Glatter, O.5    Bachinger, H.P.6    Werner, E.R.7    Schmidt, K.8    Mayer, B.9
  • 41
    • 0035709008 scopus 로고    scopus 로고
    • A rapid, simple spectrophotometric method for simultaneous detection of nitrate and nitrite
    • Miranda K.M., Espey M.G., Wink D.A. A rapid, simple spectrophotometric method for simultaneous detection of nitrate and nitrite. Nitric Oxide 2001, 5:62-71.
    • (2001) Nitric Oxide , vol.5 , pp. 62-71
    • Miranda, K.M.1    Espey, M.G.2    Wink, D.A.3
  • 42
    • 0019765114 scopus 로고
    • Preparation of blood hemoglobins of vertebrates
    • Academic Press, New York, E. Antonini, L. Rossi-Bernardi, E. Chiancone (Eds.) Methods in Enzymology
    • Riggs A. Preparation of blood hemoglobins of vertebrates. Hemoglobins and Myoglobins 1981, vol. 76:5-28. Academic Press, New York. E. Antonini, L. Rossi-Bernardi, E. Chiancone (Eds.).
    • (1981) Hemoglobins and Myoglobins , vol.76 , pp. 5-28
    • Riggs, A.1
  • 43
    • 0023692586 scopus 로고
    • A spectrophotometric method for determination of catalase activity in small tissue samples
    • Johansson L.H., Borg L.A.H. A spectrophotometric method for determination of catalase activity in small tissue samples. Anal. Biochem. 1988, 174:331-336.
    • (1988) Anal. Biochem. , vol.174 , pp. 331-336
    • Johansson, L.H.1    Borg, L.A.H.2
  • 44
    • 0032918830 scopus 로고    scopus 로고
    • Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells
    • Datta P.K., Lianos E.A. Nitric oxide induces heme oxygenase-1 gene expression in mesangial cells. Kidney Int. 1999, 55:1734-1739.
    • (1999) Kidney Int. , vol.55 , pp. 1734-1739
    • Datta, P.K.1    Lianos, E.A.2
  • 45
    • 0027358877 scopus 로고
    • Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage
    • Balla J., Jacob H.S., Balla G., Nath K., Eaton J.W., Vercellotti G.M. Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:9285-9289.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9285-9289
    • Balla, J.1    Jacob, H.S.2    Balla, G.3    Nath, K.4    Eaton, J.W.5    Vercellotti, G.M.6
  • 46
    • 1842834977 scopus 로고    scopus 로고
    • A DNA microarray study of nitric oxide-induced genes in mouse hepatocytes: implications for hepatic heme oxygenase-1 expression in ischemia/reperfusion
    • Zamora R., Vodovotz Y., Aulak K.S., Kim P.K., Kane J.M., Alarcon L., Stuehr D.J., Billiar T.R. A DNA microarray study of nitric oxide-induced genes in mouse hepatocytes: implications for hepatic heme oxygenase-1 expression in ischemia/reperfusion. Nitric Oxide 2002, 7:165-186.
    • (2002) Nitric Oxide , vol.7 , pp. 165-186
    • Zamora, R.1    Vodovotz, Y.2    Aulak, K.S.3    Kim, P.K.4    Kane, J.M.5    Alarcon, L.6    Stuehr, D.J.7    Billiar, T.R.8
  • 48
    • 0028925540 scopus 로고
    • Nitric oxide (NO) donor molecules: effect of NO release rate on vascular smooth muscle cell proliferation in vitro
    • Mooradian D.L., Hutsell T.C., Keefer L.K. Nitric oxide (NO) donor molecules: effect of NO release rate on vascular smooth muscle cell proliferation in vitro. J. Cardiovasc. Pharmacol. 1995, 25:674-678.
    • (1995) J. Cardiovasc. Pharmacol. , vol.25 , pp. 674-678
    • Mooradian, D.L.1    Hutsell, T.C.2    Keefer, L.K.3
  • 52
    • 0029763714 scopus 로고    scopus 로고
    • Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line
    • Rafferty S.P., Domachowske J.B., Malech H.L. Inhibition of hemoglobin expression by heterologous production of nitric oxide synthase in the K562 erythroleukemic cell line. Blood 1996, 88:1070-1078.
    • (1996) Blood , vol.88 , pp. 1070-1078
    • Rafferty, S.P.1    Domachowske, J.B.2    Malech, H.L.3
  • 53
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • Cooper C.E. Nitric oxide and iron proteins. Biochim. Biophys. Acta 1999, 1411:290-309.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 290-309
    • Cooper, C.E.1
  • 54
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • Kharitonov V.G., Sharma V.S., Magde D., Koesling D. Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase. Biochemistry 1997, 36:6814-6818.
    • (1997) Biochemistry , vol.36 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 56
    • 0033534474 scopus 로고    scopus 로고
    • Antifungal imidazoles block assembly of inducible NO synthase into an active dimer
    • Sennequier N., Wolan D., Stuehr D.J. Antifungal imidazoles block assembly of inducible NO synthase into an active dimer. J. Biol. Chem. 1999, 274:930-938.
    • (1999) J. Biol. Chem. , vol.274 , pp. 930-938
    • Sennequier, N.1    Wolan, D.2    Stuehr, D.J.3
  • 58
    • 0032974932 scopus 로고    scopus 로고
    • Nitric oxide-generated P420 nitric oxide synthase: characterization and roles for tetrahydrobiopterin and substrate in protecting against or reversing the P420 conversion
    • Huang L., Abu-Soud H.M., Hille R., Stuehr D.J. Nitric oxide-generated P420 nitric oxide synthase: characterization and roles for tetrahydrobiopterin and substrate in protecting against or reversing the P420 conversion. Biochemistry 1999, 38:1912-1920.
    • (1999) Biochemistry , vol.38 , pp. 1912-1920
    • Huang, L.1    Abu-Soud, H.M.2    Hille, R.3    Stuehr, D.J.4
  • 59
    • 0037418534 scopus 로고    scopus 로고
    • Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes: evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase
    • Voegtle H.L., Sono M., Adak S., Pond A.E., Tomita T., Perera R., Goodin D.B., Ikeda-Saito M., Stuehr D.J., Dawson J.H. Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes: evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase. Biochemistry 2003, 42:2475-2484.
    • (2003) Biochemistry , vol.42 , pp. 2475-2484
    • Voegtle, H.L.1    Sono, M.2    Adak, S.3    Pond, A.E.4    Tomita, T.5    Perera, R.6    Goodin, D.B.7    Ikeda-Saito, M.8    Stuehr, D.J.9    Dawson, J.H.10
  • 60
    • 61449218869 scopus 로고    scopus 로고
    • Ortiz de Montellano, P.R. Reaction of Mycobacterium tuberculosis cytochrome P450 enzymes with nitric oxide
    • Ouellet H., Lang J., Couture M. Ortiz de Montellano, P.R. Reaction of Mycobacterium tuberculosis cytochrome P450 enzymes with nitric oxide. Biochemistry 2009, 48:863-872.
    • (2009) Biochemistry , vol.48 , pp. 863-872
    • Ouellet, H.1    Lang, J.2    Couture, M.3
  • 61
    • 0029082717 scopus 로고
    • Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to its NO reduction activity
    • Shiro Y., Fujii M., Isogai Y., Adachi S., Iizuka T., Obayashi E., Makino R., Nakahara K., Shoun H. Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to its NO reduction activity. Biochemistry 1995, 34:9052-9058.
    • (1995) Biochemistry , vol.34 , pp. 9052-9058
    • Shiro, Y.1    Fujii, M.2    Isogai, Y.3    Adachi, S.4    Iizuka, T.5    Obayashi, E.6    Makino, R.7    Nakahara, K.8    Shoun, H.9
  • 63
    • 0032497407 scopus 로고    scopus 로고
    • Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase
    • Zhao Y., Hoganson C., Babcock G.T., Marletta M.A. Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase. Biochemistry 1998, 37:12458-12464.
    • (1998) Biochemistry , vol.37 , pp. 12458-12464
    • Zhao, Y.1    Hoganson, C.2    Babcock, G.T.3    Marletta, M.A.4
  • 64
    • 0037687336 scopus 로고    scopus 로고
    • YC-1 facilitates release of the proximal His residue in the NO and CO complexes of soluble guanylate cyclase
    • Makino R., Obayashi E., Homma N., Shiro Y., Hori H. YC-1 facilitates release of the proximal His residue in the NO and CO complexes of soluble guanylate cyclase. J. Biol. Chem. 2003, 278:11130-11137.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11130-11137
    • Makino, R.1    Obayashi, E.2    Homma, N.3    Shiro, Y.4    Hori, H.5
  • 65
    • 0027505784 scopus 로고
    • Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
    • Adachi S., Nagano S., Ishimori K., Watanabe Y., Morishima I., Egawa T., Kitagawa T., Makino R. Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase. Biochemistry 1993, 32:241-252.
    • (1993) Biochemistry , vol.32 , pp. 241-252
    • Adachi, S.1    Nagano, S.2    Ishimori, K.3    Watanabe, Y.4    Morishima, I.5    Egawa, T.6    Kitagawa, T.7    Makino, R.8
  • 66
    • 0032493731 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions
    • Yonetani T., Tsuneshige A., Zhou Y., Chen X. Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 1998, 273:20323-20333.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20323-20333
    • Yonetani, T.1    Tsuneshige, A.2    Zhou, Y.3    Chen, X.4
  • 68
    • 58849128622 scopus 로고    scopus 로고
    • Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization
    • Vetter S.W., Terentis A.C., Osborne R.L., Dawson J.H., Goodin D.B. Replacement of the axial histidine heme ligand with cysteine in nitrophorin 1: spectroscopic and crystallographic characterization. J. Biol. Inorg. Chem. 2009, 14:179-191.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 179-191
    • Vetter, S.W.1    Terentis, A.C.2    Osborne, R.L.3    Dawson, J.H.4    Goodin, D.B.5
  • 70
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy C.J., Gibney B.R. Heme protein assemblies. Chem. Rev. 2004, 104:617-649.
    • (2004) Chem. Rev. , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 71
    • 0032103447 scopus 로고    scopus 로고
    • Haem insertion, dimerization and reactivation of haem-free rat neuronal nitric oxide synthase
    • Hemmens B., Gorren A.C., Schmidt K., Werner E.R., Mayer B. Haem insertion, dimerization and reactivation of haem-free rat neuronal nitric oxide synthase. Biochem. J. 1998, 332:337-342.
    • (1998) Biochem. J. , vol.332 , pp. 337-342
    • Hemmens, B.1    Gorren, A.C.2    Schmidt, K.3    Werner, E.R.4    Mayer, B.5
  • 72
    • 33846491964 scopus 로고    scopus 로고
    • NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism
    • Ma X., Sayed N., Beuve A., van den Akker F. NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism. EMBO J. 2007, 26:578-588.
    • (2007) EMBO J. , vol.26 , pp. 578-588
    • Ma, X.1    Sayed, N.2    Beuve, A.3    van den Akker, F.4
  • 73
    • 34447526071 scopus 로고    scopus 로고
    • Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins
    • Landfried D.A., Vuletich D.A., Pond M.P., Lecomte J.T. Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins. Gene 2007, 398:12-28.
    • (2007) Gene , vol.398 , pp. 12-28
    • Landfried, D.A.1    Vuletich, D.A.2    Pond, M.P.3    Lecomte, J.T.4
  • 74
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: a current perspective
    • Foster M.W., Hess D.T., Stamler J.S. Protein S-nitrosylation in health and disease: a current perspective. Trends Mol. Med. 2009, 15:391-404.
    • (2009) Trends Mol. Med. , vol.15 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 75
    • 34250714956 scopus 로고    scopus 로고
    • Biochemistry of protein tyrosine nitration in cardiovascular pathology
    • Peluffo G., Radi R. Biochemistry of protein tyrosine nitration in cardiovascular pathology. Cardiovasc. Res. 2007, 75:291-302.
    • (2007) Cardiovasc. Res. , vol.75 , pp. 291-302
    • Peluffo, G.1    Radi, R.2
  • 76
    • 0031037538 scopus 로고    scopus 로고
    • Glutathione redox cycle regulates nitric oxide-mediated glyceraldehyde-3-phosphate dehydrogenase inhibition
    • Padgett C.M., Whorton A.R. Glutathione redox cycle regulates nitric oxide-mediated glyceraldehyde-3-phosphate dehydrogenase inhibition. Am. J. Physiol. 1997, 272:C99-C108.
    • (1997) Am. J. Physiol. , vol.272
    • Padgett, C.M.1    Whorton, A.R.2
  • 77
    • 20444409884 scopus 로고    scopus 로고
    • Receptor-regulated dynamic S-nitrosylation of endothelial nitric-oxide synthase in vascular endothelial cells
    • Erwin P.A., Lin A.J., Golan D.E., Michel T. Receptor-regulated dynamic S-nitrosylation of endothelial nitric-oxide synthase in vascular endothelial cells. J. Biol. Chem. 2005, 280:19888-19894.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19888-19894
    • Erwin, P.A.1    Lin, A.J.2    Golan, D.E.3    Michel, T.4
  • 78
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: enzymatic mechanisms and cellular functions
    • Benhar M., Forrester M.T., Stamler J.S. Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell. Biol. 2009, 10:721-732.
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 79
    • 3042646339 scopus 로고    scopus 로고
    • Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria
    • Koeck T., Fu X., Hazen S.L., Crabb J.W., Stuehr D.J., Aulak K.S. Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J. Biol. Chem. 2004, 279:27257-27262.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27257-27262
    • Koeck, T.1    Fu, X.2    Hazen, S.L.3    Crabb, J.W.4    Stuehr, D.J.5    Aulak, K.S.6
  • 81
    • 34547427294 scopus 로고    scopus 로고
    • Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells
    • Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A. Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:11609-11614.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 11609-11614
    • Mitchell, D.A.1    Morton, S.U.2    Fernhoff, N.B.3    Marletta, M.A.4
  • 82
    • 70349970651 scopus 로고    scopus 로고
    • S-nitrosoproteome in endothelial cells revealed by a modified biotin switch approach coupled with Western blot-based two-dimensional gel electrophoresis
    • Huang B., Liao C.L., Lin Y.P., Chen S.C., Wang D.L. S-nitrosoproteome in endothelial cells revealed by a modified biotin switch approach coupled with Western blot-based two-dimensional gel electrophoresis. J. Proteome Res. 2009, 8:4835-4843.
    • (2009) J. Proteome Res. , vol.8 , pp. 4835-4843
    • Huang, B.1    Liao, C.L.2    Lin, Y.P.3    Chen, S.C.4    Wang, D.L.5
  • 85
    • 24144487005 scopus 로고    scopus 로고
    • Angiotensin II induces tyrosine nitration and activation of ERK1/2 in vascular smooth muscle cells
    • Pinzar E., Wang T., Garrido M.R., Xu W., Levy P., Bottari S.P. Angiotensin II induces tyrosine nitration and activation of ERK1/2 in vascular smooth muscle cells. FEBS Lett. 2005, 579:5100-5104.
    • (2005) FEBS Lett. , vol.579 , pp. 5100-5104
    • Pinzar, E.1    Wang, T.2    Garrido, M.R.3    Xu, W.4    Levy, P.5    Bottari, S.P.6
  • 86
    • 33749641285 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase is required for transnitrosation of metallothionein by S-nitroso-albumin in intact rat pulmonary vascular endothelial cells
    • Zhang L.M., St.Croix C., Cao R., Wasserloos K., Watkins S.C., Stevens T., Li S., Tyurin V., Kagan V.E., Pitt B.R. Cell-surface protein disulfide isomerase is required for transnitrosation of metallothionein by S-nitroso-albumin in intact rat pulmonary vascular endothelial cells. Exp. Biol. Med. 2006, 231:1507-1515.
    • (2006) Exp. Biol. Med. , vol.231 , pp. 1507-1515
    • Zhang, L.M.1    St.Croix, C.2    Cao, R.3    Wasserloos, K.4    Watkins, S.C.5    Stevens, T.6    Li, S.7    Tyurin, V.8    Kagan, V.E.9    Pitt, B.R.10
  • 87
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • Sliskovic I., Raturi A., Mutus B. Characterization of the S-denitrosation activity of protein disulfide isomerase. J. Biol. Chem. 2005, 280:8733-8741.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 90
    • 34347218612 scopus 로고    scopus 로고
    • Activation of peroxynitrite by inducible nitric-oxide synthase: a direct source of nitrative stress
    • Maréchal A., Mattioli T.A., Stuehr D.J., Santolini J. Activation of peroxynitrite by inducible nitric-oxide synthase: a direct source of nitrative stress. J. Biol. Chem. 2007, 282:14101-14112.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14101-14112
    • Maréchal, A.1    Mattioli, T.A.2    Stuehr, D.J.3    Santolini, J.4
  • 92
    • 2942665472 scopus 로고    scopus 로고
    • Hypoxic inducible factor 1alpha, extracellular signal-regulated kinase, and p53 are regulated by distinct threshold concentrations of nitric oxide
    • Thomas D.D., Espey M.G., Ridnour L.A., Hofseth L.J., Mancardi D., Harris C.C., Wink D.A. Hypoxic inducible factor 1alpha, extracellular signal-regulated kinase, and p53 are regulated by distinct threshold concentrations of nitric oxide. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:8894-8899.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8894-8899
    • Thomas, D.D.1    Espey, M.G.2    Ridnour, L.A.3    Hofseth, L.J.4    Mancardi, D.5    Harris, C.C.6    Wink, D.A.7
  • 93
    • 0025314289 scopus 로고
    • Kupffer cell:hepatocyte cocultures release nitric oxide in response to bacterial endotoxin
    • Billiar T.R., Curran R.D., Ferrari F.K., Williams D.L., Simmons R.L. Kupffer cell:hepatocyte cocultures release nitric oxide in response to bacterial endotoxin. J. Surg. Res. 1990, 48:349-353.
    • (1990) J. Surg. Res. , vol.48 , pp. 349-353
    • Billiar, T.R.1    Curran, R.D.2    Ferrari, F.K.3    Williams, D.L.4    Simmons, R.L.5
  • 94
    • 0032701107 scopus 로고    scopus 로고
    • Regulation of induction of nitric oxide synthase and the inhibitory actions of dexamethasone in the human intestinal epithelial cell line, Caco-2: influence of cell differentiation
    • Cavicchi M., Whittle B.J. Regulation of induction of nitric oxide synthase and the inhibitory actions of dexamethasone in the human intestinal epithelial cell line, Caco-2: influence of cell differentiation. Br. J. Pharmacol. 1999, 128:705-715.
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 705-715
    • Cavicchi, M.1    Whittle, B.J.2
  • 95
    • 0028575633 scopus 로고
    • Distinct patterns of nitric oxide production in hepatic macrophages and endothelial cells following acute exposure of rats to endotoxin
    • Laskin D.L., Heck D.E., Gardner C.R., Feder L.S., Laskin J.D. Distinct patterns of nitric oxide production in hepatic macrophages and endothelial cells following acute exposure of rats to endotoxin. J. Leukoc. Biol. 1994, 56:751-758.
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 751-758
    • Laskin, D.L.1    Heck, D.E.2    Gardner, C.R.3    Feder, L.S.4    Laskin, J.D.5
  • 97
    • 0346728620 scopus 로고    scopus 로고
    • Cytokines and nitric oxide inhibit the enzyme activity of catalase but not its protein or mRNA expression in insulin-producing cells
    • Sigfrid L.A., Cunningham J.M., Beeharry N., Lortz S., Tiedge M., Lenzen S., Carlsson C., Green I.C. Cytokines and nitric oxide inhibit the enzyme activity of catalase but not its protein or mRNA expression in insulin-producing cells. J. Mol. Endocrinol. 2003, 31:509-518.
    • (2003) J. Mol. Endocrinol. , vol.31 , pp. 509-518
    • Sigfrid, L.A.1    Cunningham, J.M.2    Beeharry, N.3    Lortz, S.4    Tiedge, M.5    Lenzen, S.6    Carlsson, C.7    Green, I.C.8
  • 98
    • 0031409592 scopus 로고    scopus 로고
    • Regulation of cytochromes P450 during inflammation and infection
    • Morgan E.T. Regulation of cytochromes P450 during inflammation and infection. Drug Metab. Rev. 1997, 29:1129-1188.
    • (1997) Drug Metab. Rev. , vol.29 , pp. 1129-1188
    • Morgan, E.T.1
  • 99
    • 9444263201 scopus 로고    scopus 로고
    • Short-term inhibitory effects of nitric oxide on cytochrome P450-mediated drug metabolism: time dependency and reversibility profiles in isolated perfused rat livers
    • Vuppugalla R., Mehvar R. Short-term inhibitory effects of nitric oxide on cytochrome P450-mediated drug metabolism: time dependency and reversibility profiles in isolated perfused rat livers. Drug Metab. Dispos. 2004, 32:1446-1454.
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1446-1454
    • Vuppugalla, R.1    Mehvar, R.2
  • 101
    • 0029739154 scopus 로고    scopus 로고
    • Inhibition of cytochrome P450 enzymes by nitric oxide
    • Stadler J., Schmalix W.A., Doehmer J. Inhibition of cytochrome P450 enzymes by nitric oxide. Adv. Exp. Med. Biol. 1996, 387:187-193.
    • (1996) Adv. Exp. Med. Biol. , vol.387 , pp. 187-193
    • Stadler, J.1    Schmalix, W.A.2    Doehmer, J.3
  • 106
    • 15344349691 scopus 로고    scopus 로고
    • Nitric oxide, oxygen, and superoxide formation and consumption in macrophage cultures
    • Nalwaya N., Deen W.M. Nitric oxide, oxygen, and superoxide formation and consumption in macrophage cultures. Chem. Res. Toxicol. 2005, 18:486-493.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 486-493
    • Nalwaya, N.1    Deen, W.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.