메뉴 건너뛰기




Volumn 47, Issue 47, 2008, Pages 12371-12379

Effect of nitration on the physicochemical and kinetic features of wild-type and monotyrosine mutants of human respiratory cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BEARINGS (STRUCTURAL);

EID: 56749136365     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801329s     Document Type: Article
Times cited : (42)

References (46)
  • 1
    • 1942536167 scopus 로고    scopus 로고
    • The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases
    • Kadenbach, B., Arnold, S., Lee, I., and Hüttemann, M. (2004) The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases. Biochim. Biophys. Acta 1655, 400-408.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 400-408
    • Kadenbach, B.1    Arnold, S.2    Lee, I.3    Hüttemann, M.4
  • 2
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • Radi, R. (2004) Nitric oxide, oxidants, and protein tyrosine nitration. Proc. Natl. Acad. Sci. U.S.A. 101, 4003-4008.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 3
    • 34548451974 scopus 로고    scopus 로고
    • Reactive oxygen species in mitochondria-mediated cell death
    • Orrenius, S. (2007) Reactive oxygen species in mitochondria-mediated cell death. Drugs Metab. Rev. 39, 443-455.
    • (2007) Drugs Metab. Rev , vol.39 , pp. 443-455
    • Orrenius, S.1
  • 4
    • 0032504574 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: The role of cytochrome c
    • Cai, J., Yang, J., and Jones, D. P. (1998) Mitochondrial control of apoptosis: the role of cytochrome c. Biochim. Biophys. Acta 1366, 139-149.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 139-149
    • Cai, J.1    Yang, J.2    Jones, D.P.3
  • 5
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Daniel, N. N., and Korsmeyer, S. J. (2004) Cell death: critical control points. Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Daniel, N.N.1    Korsmeyer, S.J.2
  • 6
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome c-mediated apoptosis
    • Jiang, X., and Wang, X. (2004) Cytochrome c-mediated apoptosis. Annu. Rev. Biochem. 73, 87-106.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 7
    • 0347361495 scopus 로고    scopus 로고
    • Peroxynitrite-dependent modifications of tyrosine residues in haemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine
    • Pietraforte, D., Salzano, A. M., Marino, G., and Minetti, M. (2003) Peroxynitrite-dependent modifications of tyrosine residues in haemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine. Amino Acids 25, 341-350.
    • (2003) Amino Acids , vol.25 , pp. 341-350
    • Pietraforte, D.1    Salzano, A.M.2    Marino, G.3    Minetti, M.4
  • 9
    • 0035369688 scopus 로고    scopus 로고
    • Site-selective nitration of tyrosine in human serum albumin by peroxynitrite
    • Jiao, K., Mandapati, S., Skipper, P. L., Tannenbaum, S. R., and Wishnok, J. S. (2001) Site-selective nitration of tyrosine in human serum albumin by peroxynitrite. Anal. Biochem. 293, 43-52.
    • (2001) Anal. Biochem , vol.293 , pp. 43-52
    • Jiao, K.1    Mandapati, S.2    Skipper, P.L.3    Tannenbaum, S.R.4    Wishnok, J.S.5
  • 10
    • 37249051057 scopus 로고    scopus 로고
    • Peroxynitrite inactivation of human cytochrome P-450s 2B6 and 2E1: Heme modification and site-specific nitrotyrosine formation
    • Lin, H. L., Myshkin, E., Waskell, L., and Hollenberg, P. F. (2007) Peroxynitrite inactivation of human cytochrome P-450s 2B6 and 2E1: heme modification and site-specific nitrotyrosine formation. Chem. Res. Toxicol. 20, 1612-1622.
    • (2007) Chem. Res. Toxicol , vol.20 , pp. 1612-1622
    • Lin, H.L.1    Myshkin, E.2    Waskell, L.3    Hollenberg, P.F.4
  • 11
    • 0346218261 scopus 로고    scopus 로고
    • Cytochrome c: A catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration
    • Castro, L., Eiserich, J. P., Sweeney, S., Radi, R., and Freeman, B. A. (2004) Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration. Arch. Biochem. Biophys. 421, 99-107.
    • (2004) Arch. Biochem. Biophys , vol.421 , pp. 99-107
    • Castro, L.1    Eiserich, J.P.2    Sweeney, S.3    Radi, R.4    Freeman, B.A.5
  • 12
    • 0037352488 scopus 로고    scopus 로고
    • Tyrosine-nitration of caspase 3 and cytochrome c does not suppress apoptosis induction in squamous cell carcinoma cells
    • Ueta, E., Kamatani, T., Yamamoto, T., and Osaki, T. (2003) Tyrosine-nitration of caspase 3 and cytochrome c does not suppress apoptosis induction in squamous cell carcinoma cells. Int. J. Cancer 103, 717-722.
    • (2003) Int. J. Cancer , vol.103 , pp. 717-722
    • Ueta, E.1    Kamatani, T.2    Yamamoto, T.3    Osaki, T.4
  • 13
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosylation of cytochrome c during apoptosis
    • Schonhoff, C. M., Gaston, B., and Mannick, J. B. (2003) Nitrosylation of cytochrome c during apoptosis. J. Biol. Chem. 278, 18265-18270.
    • (2003) J. Biol. Chem , vol.278 , pp. 18265-18270
    • Schonhoff, C.M.1    Gaston, B.2    Mannick, J.B.3
  • 14
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabó, C., Ischiropoulos, H., and Radi, R. (2007) Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nature 6, 662-680.
    • (2007) Nature , vol.6 , pp. 662-680
    • Szabó, C.1    Ischiropoulos, H.2    Radi, R.3
  • 16
    • 27944453616 scopus 로고    scopus 로고
    • Biochemical properties of cytochrome c nitrated by peroxynitrite
    • Jang, B., and Han, S. (2006) Biochemical properties of cytochrome c nitrated by peroxynitrite. Biochimie 88, 53-58.
    • (2006) Biochimie , vol.88 , pp. 53-58
    • Jang, B.1    Han, S.2
  • 17
    • 10644249922 scopus 로고    scopus 로고
    • Native, not nitrated, cytochrome c and mitochondria-derived peroxide drive osteoclast apoptosis
    • Oursler, M. J., Bradley, E. W., Elfering, S. L., and Giulivi, C. (2005) Native, not nitrated, cytochrome c and mitochondria-derived peroxide drive osteoclast apoptosis. Am. J. Physiol. Cell Physiol. 288, C156-C168.
    • (2005) Am. J. Physiol. Cell Physiol , vol.288
    • Oursler, M.J.1    Bradley, E.W.2    Elfering, S.L.3    Giulivi, C.4
  • 18
    • 33846046537 scopus 로고    scopus 로고
    • Nitration of specific tyrosine residues of cytochrome c is associated with caspase-cascade inactivation
    • Nakagawa, H., Komai, N., Takusagawa, M., Miura, Y., Toda, T., Miyata, N., Ozawa, T., and Ikota, N. (2007) Nitration of specific tyrosine residues of cytochrome c is associated with caspase-cascade inactivation. Biol. Pharm. Bull. 30, 15-20.
    • (2007) Biol. Pharm. Bull , vol.30 , pp. 15-20
    • Nakagawa, H.1    Komai, N.2    Takusagawa, M.3    Miura, Y.4    Toda, T.5    Miyata, N.6    Ozawa, T.7    Ikota, N.8
  • 19
    • 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., and Aulak, K. S. (2004) Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J. Biol. Chem. 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
  • 22
    • 18144362519 scopus 로고    scopus 로고
    • Rapid electrostatic evolution at the binding site for cytochrome c on cytochrome c oxidase in anthropoid primates
    • Schmidt, T. R., Wildman, D. E., Uddin, M., Opazo, J. C., Goodman, M., and Grossman, L. I. (2005) Rapid electrostatic evolution at the binding site for cytochrome c on cytochrome c oxidase in anthropoid primates. Proc. Natl. Acad. Sci. U.S.A. 102, 6379-6384.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6379-6384
    • Schmidt, T.R.1    Wildman, D.E.2    Uddin, M.3    Opazo, J.C.4    Goodman, M.5    Grossman, L.I.6
  • 23
    • 52049092730 scopus 로고    scopus 로고
    • Nitrocytochrome c: Synthesis, purification, and functional studies
    • Souza, J. M., Castro, C., Cassina, A. M., Batthyány, C., and Radi, R. (2008) Nitrocytochrome c: synthesis, purification, and functional studies. Methods Enzymol. 441, 197-215.
    • (2008) Methods Enzymol , vol.441 , pp. 197-215
    • Souza, J.M.1    Castro, C.2    Cassina, A.M.3    Batthyány, C.4    Radi, R.5
  • 25
    • 33646241041 scopus 로고    scopus 로고
    • Direct inhibition of cytochrome c-induced caspase activation in vitro by Toxoplasma gondii reveals novel mechanisms of interference with host cell apoptosis
    • Keller, P., Schaumburg, F., Fischer, S. F., Häcker, G., Gross, U., and Lüder, C. G. (2006) Direct inhibition of cytochrome c-induced caspase activation in vitro by Toxoplasma gondii reveals novel mechanisms of interference with host cell apoptosis. FEMS Microbiol. Lett. 258, 312-319.
    • (2006) FEMS Microbiol. Lett , vol.258 , pp. 312-319
    • Keller, P.1    Schaumburg, F.2    Fischer, S.F.3    Häcker, G.4    Gross, U.5    Lüder, C.G.6
  • 27
    • 0028816957 scopus 로고
    • Integral cytochrome-c oxidase. Preparation and progress towards a three-dimensional crystallization
    • Soulimane, T., and Buse, G. (1995) Integral cytochrome-c oxidase. Preparation and progress towards a three-dimensional crystallization. Eur. J. Biochem. 227, 588-595.
    • (1995) Eur. J. Biochem , vol.227 , pp. 588-595
    • Soulimane, T.1    Buse, G.2
  • 28
    • 0017727697 scopus 로고
    • An infrared study of CO binding to heart cytohrome c oxidase and hemoglobin A
    • Yoshikawa, S., Choc, M. G., O'Toole, M. C., and Caughey, W. S. (1977) An infrared study of CO binding to heart cytohrome c oxidase and hemoglobin A. J. Biol. Chem. 252, 5498-5508.
    • (1977) J. Biol. Chem , vol.252 , pp. 5498-5508
    • Yoshikawa, S.1    Choc, M.G.2    O'Toole, M.C.3    Caughey, W.S.4
  • 29
    • 0014194993 scopus 로고
    • Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins
    • Sokolovsky, M., Riordan, J. F., and Vallee, B. L. (1967) Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins. Biochem. Biophys. Res. Commun. 27, 20-25.
    • (1967) Biochem. Biophys. Res. Commun , vol.27 , pp. 20-25
    • Sokolovsky, M.1    Riordan, J.F.2    Vallee, B.L.3
  • 30
    • 0028820053 scopus 로고
    • Use of flavin photochemistry to probe intraprotein and interprotein electron transfer mechanisms
    • Tollin, G. (1995) Use of flavin photochemistry to probe intraprotein and interprotein electron transfer mechanisms. J. Bioenerg. Biomembr. 27, 303-309.
    • (1995) J. Bioenerg. Biomembr , vol.27 , pp. 303-309
    • Tollin, G.1
  • 31
    • 0014674066 scopus 로고
    • Electron transport systems of Rhizobium japonicum. II. Rhizobium haemoglobin, cytochromes and oxidases in free-living (cultured) cells
    • Appleby, C. A. (1969) Electron transport systems of Rhizobium japonicum. II. Rhizobium haemoglobin, cytochromes and oxidases in free-living (cultured) cells. Biochim. Biophys. Acta 172, 88-105.
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 88-105
    • Appleby, C.A.1
  • 32
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 282, 252-260.
    • (2000) Anal. Biochem , vol.282 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0028500694 scopus 로고
    • Laser flash-induced photoreduction of photosynthetic ferredoxins and flavodoxin by 5-deazariboflavin and by a viologen analogue
    • Navarro, J. A., Hervás, M., Pueyo, J. J., Medina, M., Gómez-Moreno, C., De la Rosa, M. A., and Tollin, G. (1994) Laser flash-induced photoreduction of photosynthetic ferredoxins and flavodoxin by 5-deazariboflavin and by a viologen analogue. Photochem. Photobiol. 60, 231-236.
    • (1994) Photochem. Photobiol , vol.60 , pp. 231-236
    • Navarro, J.A.1    Hervás, M.2    Pueyo, J.J.3    Medina, M.4    Gómez-Moreno, C.5    De la Rosa, M.A.6    Tollin, G.7
  • 34
    • 0028670747 scopus 로고
    • A "parallel plate" electrostatic model for bimolecular rate constants applied to electron transfer proteins
    • Watkins, J. A., Cusanovich, M. A., Meyer, T. E., and Tollin, G. (1994) A "parallel plate" electrostatic model for bimolecular rate constants applied to electron transfer proteins. Protein Sci. 3, 2104-2114.
    • (1994) Protein Sci , vol.3 , pp. 2104-2114
    • Watkins, J.A.1    Cusanovich, M.A.2    Meyer, T.E.3    Tollin, G.4
  • 35
    • 0026016270 scopus 로고
    • Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase
    • Hazzard, J. T., Rong, S. Y., and Tollin, G. (1991) Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase. Biochemistry 30, 213-222.
    • (1991) Biochemistry , vol.30 , pp. 213-222
    • Hazzard, J.T.1    Rong, S.Y.2    Tollin, G.3
  • 37
    • 0027319734 scopus 로고
    • Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin
    • Meyer, T. E., Zhao, Z. G., Cusanovich, M. A., and Tollin, G. (1993) Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin. Biochemistry 32, 4552-4559.
    • (1993) Biochemistry , vol.32 , pp. 4552-4559
    • Meyer, T.E.1    Zhao, Z.G.2    Cusanovich, M.A.3    Tollin, G.4
  • 38
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., and Lesnefsky, E. J. (2003) Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 278, 36027-36031.
    • (2003) J. Biol. Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 39
    • 0021770911 scopus 로고
    • Electron-transfer reactions of photoreduced flavin analogues with c-type cytochromes: Quantitation of steric and electrostatic factors
    • Meyer, T. E., Watkins, J. A., Przysiecki, C. T., Tollin, G., and Cusanovich, M. A. (1984) Electron-transfer reactions of photoreduced flavin analogues with c-type cytochromes: quantitation of steric and electrostatic factors. Biochemistry 23, 4761-4767.
    • (1984) Biochemistry , vol.23 , pp. 4761-4767
    • Meyer, T.E.1    Watkins, J.A.2    Przysiecki, C.T.3    Tollin, G.4    Cusanovich, M.A.5
  • 41
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfer amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms
    • Hope, A. B. (2000) Electron transfer amongst cytochrome f, plastocyanin and photosystem I: kinetics and mechanisms. Biochim. Biophys. Acta 1456, 5-26.
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 43
    • 0035918306 scopus 로고    scopus 로고
    • A Mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1
    • Yu, T., Wang, X., Puning-Koch, C., Wei, Y., and McLendon, G. L. (2001) A Mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1. J. Biol. Chem. 276, 13034-13038.
    • (2001) J. Biol. Chem , vol.276 , pp. 13034-13038
    • Yu, T.1    Wang, X.2    Puning-Koch, C.3    Wei, Y.4    McLendon, G.L.5
  • 44
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan, D., Jiang, X., Morgan, D. G., Heuser, J. E., Wang, X., and Akey, C. W. (2002) Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9, 423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 45
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • Bao, Q., and Shi, Y. (2007) Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ. 14, 56-65.
    • (2007) Cell Death Differ , vol.14 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 46
    • 27644505459 scopus 로고    scopus 로고
    • Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1
    • Kim, H. E., Du, F., Fang, M., and Wang, X. (2005) Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc. Natl. Acad. Sci. U.S.A. 102, 17545-17550.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 17545-17550
    • Kim, H.E.1    Du, F.2    Fang, M.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.