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Volumn 49, Issue 41, 2010, Pages 8857-8872

Unprecedented peroxidase-like activity of rhodnius prolixus nitrophorin 2: Identification of the [FeIV=O Por•]+ and [FeIV=O Por](Tyr38•) intermediates and their role(s) in substrate oxidation

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION; ABSORPTION SPECTROSCOPY; AMINO ACIDS; ANTIFERROMAGNETISM; BODY FLUIDS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HYDROGEN; HYDROGEN BONDS; HYDROGEN PEROXIDE; NITRIC OXIDE; OXIDATION; PARAMAGNETIC RESONANCE; PORPHYRINS;

EID: 77957898207     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100499a     Document Type: Article
Times cited : (14)

References (72)
  • 3
    • 33845643031 scopus 로고    scopus 로고
    • Two alternative substrate paths for compound i formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei
    • Deemagarn, T., Wiseman, B., Carpena, X., Ivancich, A., Fita, I., and Loewen, P. C. (2007) Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei Proteins 66, 219-228
    • (2007) Proteins , vol.66 , pp. 219-228
    • Deemagarn, T.1    Wiseman, B.2    Carpena, X.3    Ivancich, A.4    Fita, I.5    Loewen, P.C.6
  • 4
    • 72049111244 scopus 로고    scopus 로고
    • Prostaglandin H synthase: Resolved and unresolved mechanistic issues
    • Tsai, A.-L. and Kulmacz, R. J. (2010) Prostaglandin H synthase: Resolved and unresolved mechanistic issues Arch. Biochem. Biophys. 493, 103-124
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 103-124
    • Tsai, A.-L.1    Kulmacz, R.J.2
  • 5
    • 37549012584 scopus 로고    scopus 로고
    • •] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: Reactivity toward isoniazid
    • •] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: Reactivity toward isoniazid J. Am. Chem. Soc. 129, 15954-15963
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15954-15963
    • Singh, R.1    Switala, J.2    Loewen, P.C.3    Ivancich, A.4
  • 6
    • 77953648254 scopus 로고    scopus 로고
    • A Radical on the Met-Tyr-Trp Modification Required for Catalase Activity in Catalase-Peroxidase Is Established by Isotopic Labeling and Site-Directed Mutagenesis
    • Zhao, X., Suarez, J., Khajo, A., Yu, S., Metlistsky, L., and Magliozzo, R. (2010) A Radical on the Met-Tyr-Trp Modification Required for Catalase Activity in Catalase-Peroxidase Is Established by Isotopic Labeling and Site-Directed Mutagenesis J. Am. Chem. Soc. 131, 8268-8269
    • (2010) J. Am. Chem. Soc. , vol.131 , pp. 8268-8269
    • Zhao, X.1    Suarez, J.2    Khajo, A.3    Yu, S.4    Metlistsky, L.5    Magliozzo, R.6
  • 8
    • 35448933305 scopus 로고    scopus 로고
    • Nitric oxide-releasing heme proteins from the saliva of the blood-sucking insect Rhodnius prolixus
    • In (, Eds.) Vol., Chapter 5, pp - 358, Academic Press, San Diego.
    • Walker, F. A. and Montfort, W. R. (2001) Nitric oxide-releasing heme proteins from the saliva of the blood-sucking insect Rhodnius prolixus. In Advances in Inorganic Chemistry (Mauk, A. G., and and Sykes, A. G., Eds.) Vol. 51, Chapter 5, pp 295 - 358, Academic Press, San Diego.
    • (2001) Advances in Inorganic Chemistry , vol.51 , pp. 295
    • Walker, F.A.1    Montfort, W.R.2    Mauk, A.G.3    Sykes, A.G.4
  • 11
    • 0034730723 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 2
    • Andersen, J. F. and Montfort, W. R. (2000) The crystal structure of nitrophorin 2 J. Biol. Chem. 275, 30496-30503
    • (2000) J. Biol. Chem. , vol.275 , pp. 30496-30503
    • Andersen, J.F.1    Montfort, W.R.2
  • 12
    • 77957897072 scopus 로고    scopus 로고
    • PDB entries 1PEE, 1PM1, 1T68, 2A3F, 2ACP, 2AH7, 2AL0, 2ALL, 2AMM, 2ASN, 2EU7, 2HYS, and 2GTF available, manuscript in preparation.
    • Weichsel, A., Berry, R. E., Zhang, H., Walker, F. A., and Montfort, W. R. (1999-2002) PDB entries 1PEE, 1PM1, 1T68, 2A3F, 2ACP, 2AH7, 2AL0, 2ALL, 2AMM, 2ASN, 2EU7, 2HYS, and 2GTF available, manuscript in preparation.
    • (1999)
    • Weichsel, A.1    Berry, R.E.2    Zhang, H.3    Walker, F.A.4    Montfort, W.R.5
  • 13
    • 0027213409 scopus 로고
    • Reversible binding of nitric oxide by a salivary nitrosylheme protein from the blood sucking insect, Rhodnius prolixus
    • Ribeiro, J. M. C., Hazzard, J. M. H., Nussenzveig, R., Champagne, D., and Walker, F. A. (1993) Reversible binding of nitric oxide by a salivary nitrosylheme protein from the blood sucking insect, Rhodnius prolixus Science 260, 539-541
    • (1993) Science , vol.260 , pp. 539-541
    • Ribeiro, J.M.C.1    Hazzard, J.M.H.2    Nussenzveig, R.3    Champagne, D.4    Walker, F.A.5
  • 15
    • 0033550489 scopus 로고    scopus 로고
    • Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of a blood-sucking insect, Rhodnius prolixus
    • Ding, X. D., Weichsel, A., Andersen, J. F., Shokhireva, T. K., Balfour, C., Pierik, A. J., Averill, B. A., Montfort, W. R., and Walker, F. A. (1999) Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of a blood-sucking insect, Rhodnius prolixus J. Am. Chem. Soc. 121, 128-138
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 128-138
    • Ding, X.D.1    Weichsel, A.2    Andersen, J.F.3    Shokhireva, T.K.4    Balfour, C.5    Pierik, A.J.6    Averill, B.A.7    Montfort, W.R.8    Walker, F.A.9
  • 16
    • 0032532483 scopus 로고    scopus 로고
    • The crystal structure of nitrophorin 4 at 1.5 Å resolution: Transport of nitric oxide by a lipocalin-based heme protein
    • Andersen, J. F., Weichsel, A., Balfour, C. A., Champagne, D. E., and Montfort, W. R. (1998) The crystal structure of nitrophorin 4 at 1.5 Å resolution: Transport of nitric oxide by a lipocalin-based heme protein Structure 6, 1315-1327
    • (1998) Structure , vol.6 , pp. 1315-1327
    • Andersen, J.F.1    Weichsel, A.2    Balfour, C.A.3    Champagne, D.E.4    Montfort, W.R.5
  • 17
    • 0033918403 scopus 로고    scopus 로고
    • Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial
    • Weichsel, A., Andersen, J. F., Roberts, S. A., and Montfort, W. R. (2000) Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial Nat. Struct. Biol. 7, 551-554
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 551-554
    • Weichsel, A.1    Andersen, J.F.2    Roberts, S.A.3    Montfort, W.R.4
  • 18
    • 0035949448 scopus 로고    scopus 로고
    • Ligand-induced heme ruffling and bent NO geometry in ultra-high resolution structures of nitrophorin 4
    • Roberts, S. A., Weichsel, A., Qiu, Y., Shelnutt, J. A., Walker, F. A., and Montfort, W. R. (2001) Ligand-induced heme ruffling and bent NO geometry in ultra-high resolution structures of nitrophorin 4 Biochemistry 40, 11327-11337
    • (2001) Biochemistry , vol.40 , pp. 11327-11337
    • Roberts, S.A.1    Weichsel, A.2    Qiu, Y.3    Shelnutt, J.A.4    Walker, F.A.5    Montfort, W.R.6
  • 19
    • 2542528641 scopus 로고    scopus 로고
    • Role of binding site loops in controlling nitric oxide release: Structure and kinetics of mutant forms of nitrophorin 4
    • Maes, E. M., Weichsel, A., Andersen, J. F., Shepley, D., and Montfort, W. R. (2004) Role of binding site loops in controlling nitric oxide release: Structure and kinetics of mutant forms of nitrophorin 4 Biochemistry 43, 6679-6690
    • (2004) Biochemistry , vol.43 , pp. 6679-6690
    • Maes, E.M.1    Weichsel, A.2    Andersen, J.F.3    Shepley, D.4    Montfort, W.R.5
  • 20
    • 25644434241 scopus 로고    scopus 로고
    • Ultrahigh resolution structures of nitrophorin 4: Heme distortion in ferrous CO and NO complexes
    • Maes, E. M., Roberts, S. A., Weichsel, A., and Montfort, W. R. (2005) Ultrahigh resolution structures of nitrophorin 4: Heme distortion in ferrous CO and NO complexes Biochemistry 44, 12690-12699
    • (2005) Biochemistry , vol.44 , pp. 12690-12699
    • Maes, E.M.1    Roberts, S.A.2    Weichsel, A.3    Montfort, W.R.4
  • 21
    • 0030239470 scopus 로고    scopus 로고
    • Salivary thiol oxidase activity of Rhodnius prolixus
    • Ribeiro, J. M. C. (1996) Salivary thiol oxidase activity of Rhodnius prolixus Insect Biochem. Mol. Biol. 26, 899-905
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 899-905
    • Ribeiro, J.M.C.1
  • 23
    • 0032408604 scopus 로고    scopus 로고
    • Rhodnius prolixus salivary nitrophorins display heme-peroxidase activity
    • Ribeiro, J. M. C. (1998) Rhodnius prolixus salivary nitrophorins display heme-peroxidase activity Insect Biochem. Mol. Biol. 28, 1051-1057
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 1051-1057
    • Ribeiro, J.M.C.1
  • 25
    • 0001393113 scopus 로고
    • Models for peroxidase compound I: Generation and spectroscopic characterization of new oxoferryl porphyrin cation radical species
    • Mandon, D., Weiss, R., Jayaraj, K., Gold, A., Terner, J., Bill, E., and Trautwein, A. X. (1992) Models for peroxidase compound I: Generation and spectroscopic characterization of new oxoferryl porphyrin cation radical species Inorg. Chem. 31, 4404-4409
    • (1992) Inorg. Chem. , vol.31 , pp. 4404-4409
    • Mandon, D.1    Weiss, R.2    Jayaraj, K.3    Gold, A.4    Terner, J.5    Bill, E.6    Trautwein, A.X.7
  • 27
    • 0000169326 scopus 로고    scopus 로고
    • ESR studies of A1u and A2u oxoiron(IV) porphyrin γ-cation radical complexes. Spin coupling between ferryl iron and A1u/A2u orbitals
    • Fujii, H., Yoshimura, T., and Kamada, H. (1996) ESR studies of A1u and A2u oxoiron(IV) porphyrin γ-cation radical complexes. Spin coupling between ferryl iron and A1u/A2u orbitals Inorg. Chem. 35, 2373-2377
    • (1996) Inorg. Chem. , vol.35 , pp. 2373-2377
    • Fujii, H.1    Yoshimura, T.2    Kamada, H.3
  • 29
    • 0037389596 scopus 로고    scopus 로고
    • Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure and dynamics of axial ligand complexes
    • Shokhireva, T. Kh., Berry, R. E., Uno, E., Balfour, C. A., Zhang, H., and Walker, F. A. (2003) Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure and dynamics of axial ligand complexes Proc. Natl. Acad. Sci. U.S.A. 100, 3778-3783
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3778-3783
    • Shokhireva, T.Kh.1    Berry, R.E.2    Uno, E.3    Balfour, C.A.4    Zhang, H.5    Walker, F.A.6
  • 30
    • 34250177977 scopus 로고    scopus 로고
    • The effect of the N-terminus on heme cavity structure, ligand equilibrium and rate constants, and reduction potentials of nitrophorin 2 from Rhodnius prolixus
    • Berry, R. E., Shokhireva, T. K., Filippov, I., Shokhirev, M. N., Zhang, H., and Walker, F. A. (2007) The effect of the N-terminus on heme cavity structure, ligand equilibrium and rate constants, and reduction potentials of nitrophorin 2 from Rhodnius prolixus Biochemistry 46, 6830-6843
    • (2007) Biochemistry , vol.46 , pp. 6830-6843
    • Berry, R.E.1    Shokhireva, T.K.2    Filippov, I.3    Shokhirev, M.N.4    Zhang, H.5    Walker, F.A.6
  • 31
    • 0028947447 scopus 로고
    • Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus
    • Champagne, D. E., Nussenzveig, R. H., and Ribeiro, J. M. C. (1995) Purification, partial characterization, and cloning of nitric oxide-carrying heme proteins (nitrophorins) from salivary glands of the blood-sucking insect Rhodnius prolixus J. Biol. Chem. 270, 8691-8695
    • (1995) J. Biol. Chem. , vol.270 , pp. 8691-8695
    • Champagne, D.E.1    Nussenzveig, R.H.2    Ribeiro, J.M.C.3
  • 35
    • 0034814655 scopus 로고    scopus 로고
    • Multifrequency high-field EPR study of the tryptophanyl and tyrosyl radical intermediates in wild-type and the W191G mutant of cytochrome c peroxidase
    • Ivancich, A., Dorlet, P., Goodin, D. B., and Un, S. (2001) Multifrequency high-field EPR study of the tryptophanyl and tyrosyl radical intermediates in wild-type and the W191G mutant of cytochrome c peroxidase J. Am. Chem. Soc. 123, 5050-5058
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5050-5058
    • Ivancich, A.1    Dorlet, P.2    Goodin, D.B.3    Un, S.4
  • 36
    • 51849113762 scopus 로고    scopus 로고
    • Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: Investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy
    • Fielding, A. J., Singh, R., Boscolo, B., Ghibaudi, E. M., and Ivancich, A. (2008) Intramolecular electron transfer versus substrate oxidation in lactoperoxidase: Investigation of radical intermediates by stopped-flow absorption spectrophotometry and (9-285 GHz) electron paramagnetic resonance spectroscopy Biochemistry 47, 9781-9792
    • (2008) Biochemistry , vol.47 , pp. 9781-9792
    • Fielding, A.J.1    Singh, R.2    Boscolo, B.3    Ghibaudi, E.M.4    Ivancich, A.5
  • 37
    • 0030835382 scopus 로고    scopus 로고
    • EPR investigation of compound i in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates
    • Ivancich, A., Jouve, H. M., Sartot, B., and Gaillard, J. (1997) EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates Biochemistry 36, 9356-9364
    • (1997) Biochemistry , vol.36 , pp. 9356-9364
    • Ivancich, A.1    Jouve, H.M.2    Sartot, B.3    Gaillard, J.4
  • 38
    • 70349522119 scopus 로고    scopus 로고
    • Spectroscopic evidence for an engineered catalytically-active Trp radical that recreates the unique reactivity of lignin peroxidase
    • Smith, A. T., Doyle, W. A., Dorlet, P., and Ivancich, A. (2009) Spectroscopic evidence for an engineered catalytically-active Trp radical that recreates the unique reactivity of lignin peroxidase Proc. Natl. Acad. Sci. U.S.A. 106, 16084-16089
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16084-16089
    • Smith, A.T.1    Doyle, W.A.2    Dorlet, P.3    Ivancich, A.4
  • 39
    • 70349575359 scopus 로고    scopus 로고
    • 13C NMR spectroscopic studies of the ferriheme resonances of the low-spin imidazole, histamine and cyanide complexes of wt nitrophorin 2 and NP2(V24E) as a function of pH
    • 13C NMR spectroscopic studies of the ferriheme resonances of the low-spin imidazole, histamine and cyanide complexes of wt nitrophorin 2 and NP2(V24E) as a function of pH J. Biol. Inorg. Chem. 14, 1077-1095
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 1077-1095
    • Yang, F.1    Knipp, M.2    Berry, R.E.3    Shokhireva, T.K.4    Zhang, H.5    Walker, F.A.6
  • 40
    • 0025200713 scopus 로고
    • Evidence for nitroxyl in the catalase-mediated bioactivation of the alcohol deterrent agent cyanamide
    • Nagasawa, H. T., DeMaster, E. G., Redfern, B., Shirota, F. N., and Goon, D. J. W. (1990) Evidence for nitroxyl in the catalase-mediated bioactivation of the alcohol deterrent agent cyanamide J. Med. Chem. 33, 3120-3122
    • (1990) J. Med. Chem. , vol.33 , pp. 3120-3122
    • Nagasawa, H.T.1    Demaster, E.G.2    Redfern, B.3    Shirota, F.N.4    Goon, D.J.W.5
  • 41
    • 0026641098 scopus 로고
    • An N-hydroxylated derivative of cyanamide that inhibits yeast aldehyde dehydrogenase
    • Nagasawa, H. T., Lee, M. J. C., Kwon, C.-H., Shirota, F. N., and DeMaster, E. G. (1992) An N-hydroxylated derivative of cyanamide that inhibits yeast aldehyde dehydrogenase Alcohol 9, 349-353
    • (1992) Alcohol , vol.9 , pp. 349-353
    • Nagasawa, H.T.1    Lee, M.J.C.2    Kwon, C.-H.3    Shirota, F.N.4    Demaster, E.G.5
  • 42
    • 0037279802 scopus 로고    scopus 로고
    • The nitric oxide producing reactions of hydroxyurea
    • King, S. B. (2003) The nitric oxide producing reactions of hydroxyurea Curr. Med. Chem. 10, 437-452
    • (2003) Curr. Med. Chem. , vol.10 , pp. 437-452
    • King, S.B.1
  • 43
    • 65349191154 scopus 로고    scopus 로고
    • The effect of mutation of carboxylate side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine and imidazole complexes
    • Berry, R. E., Shokhirev, M. N., Ho, A. Y. W., Yang, F., Shokhireva, T. K., Zhang, H., Weichsel, A., Montfort, W. R., and Walker, F. A. (2009) The effect of mutation of carboxylate side-chain amino acids near the heme on the midpoint potentials and ligand binding constants of nitrophorin 2 and its NO, histamine and imidazole complexes J. Am. Chem. Soc. 131, 2313-2327
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2313-2327
    • Berry, R.E.1    Shokhirev, M.N.2    Ho, A.Y.W.3    Yang, F.4    Shokhireva, T.K.5    Zhang, H.6    Weichsel, A.7    Montfort, W.R.8    Walker, F.A.9
  • 44
    • 0002159495 scopus 로고    scopus 로고
    • Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach
    • Astashkin, A. V., Raitsimring, A. M., and Walker, F. A. (1999) Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach Chem. Phys. Lett. 306, 9-17
    • (1999) Chem. Phys. Lett. , vol.306 , pp. 9-17
    • Astashkin, A.V.1    Raitsimring, A.M.2    Walker, F.A.3
  • 45
    • 77956900727 scopus 로고    scopus 로고
    • Structure-function relationships in heme peroxidases: New insights from electronic absorption, resonance Raman and multifrequency electron paramagnetic resonance spectroscopies
    • In (, Eds.) Vol., Chapter 31, pp - 453, World Scientific, Hackensack, NJ.
    • Smulevich, G., Feis, A., Howes, B. D., and Ivancich, A. (2010) Structure-function relationships in heme peroxidases: New insights from electronic absorption, resonance Raman and multifrequency electron paramagnetic resonance spectroscopies. In The Handbook of Porphyrin Science (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 6, Chapter 31, pp 367 - 453, World Scientific, Hackensack, NJ.
    • (2010) The Handbook of Porphyrin Science , vol.6 , pp. 367
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3    Ivancich, A.4    Kadish, K.M.5    Smith, K.M.6    Guilard, R.7
  • 46
    • 0028913020 scopus 로고
    • Identification of a porphyrin γ-cation radical in ascorbate peroxidase Compound i
    • Patterson, W. R., Poulos, T. L., and Goodin, D. B. (1995) Identification of a porphyrin γ-cation radical in ascorbate peroxidase Compound I Biochemistry 34, 4342-4345
    • (1995) Biochemistry , vol.34 , pp. 4342-4345
    • Patterson, W.R.1    Poulos, T.L.2    Goodin, D.B.3
  • 47
    • 0035849509 scopus 로고    scopus 로고
    • Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes
    • Ivancich, A., Mazza, G., and Desbois, A. (2001) Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes Biochemistry 40, 6860-6866
    • (2001) Biochemistry , vol.40 , pp. 6860-6866
    • Ivancich, A.1    Mazza, G.2    Desbois, A.3
  • 48
    • 0242414727 scopus 로고    scopus 로고
    • Protein-based radicals in the catalase-peroxidase of Synechocystis PCC6803: A multifrequency EPR investigation of wild-type and variants on the environment of the heme active site
    • Ivancich, A., Jakopitsch, C., Auer, M., Un, S., and Obinger, C. (2003) Protein-based radicals in the catalase-peroxidase of Synechocystis PCC6803: A multifrequency EPR investigation of wild-type and variants on the environment of the heme active site J. Am. Chem. Soc. 125, 14093-14102
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14093-14102
    • Ivancich, A.1    Jakopitsch, C.2    Auer, M.3    Un, S.4    Obinger, C.5
  • 49
    • 33646146725 scopus 로고    scopus 로고
    • Identification of Trp106 as the tryptophanyl radical intermediate in Synechocystis PCC6803 catalase-peroxidase by multifrequency electron paramagnetic resonance spectroscopy
    • Jakopitsch, C., Obinger, C., Un, S., and Ivancich, A. (2006) Identification of Trp106 as the tryptophanyl radical intermediate in Synechocystis PCC6803 catalase-peroxidase by multifrequency electron paramagnetic resonance spectroscopy J. Inorg. Biochem. 100, 1091-1099
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 1091-1099
    • Jakopitsch, C.1    Obinger, C.2    Un, S.3    Ivancich, A.4
  • 50
    • 67650545661 scopus 로고    scopus 로고
    • •] intermediates in the peroxidase reaction of Bulkholderia pseudomallei catalase-peroxidase: A multifrequency EPR spectroscopy investigation
    • •] intermediates in the peroxidase reaction of Bulkholderia pseudomallei catalase-peroxidase: A multifrequency EPR spectroscopy investigation J. Am. Chem. Soc. 131, 8557-8563
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8557-8563
    • Colin, J.1    Wiseman, B.2    Switala, J.3    Loewen, P.C.4    Ivancich, A.5
  • 52
    • 0026625050 scopus 로고
    • X-ray crystal structure of canine myeloperoxidase at 3 Å resolution
    • Zheng, J. and Fenna, R. E. (1992) X-ray crystal structure of canine myeloperoxidase at 3 Å resolution J. Mol. Biol. 226, 185-207
    • (1992) J. Mol. Biol. , vol.226 , pp. 185-207
    • Zheng, J.1    Fenna, R.E.2
  • 53
    • 0027957704 scopus 로고
    • Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 Å resolution: Structural comparisons with the lignin and cytochrome c peroxidases
    • Kunishima, N., Fukuyama, K., Matsubara, H., Hatanaka, H., Shibano, Y., and Amachi, T. (1994) Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 Å resolution: Structural comparisons with the lignin and cytochrome c peroxidases J. Mol. Biol. 235, 331-344
    • (1994) J. Mol. Biol. , vol.235 , pp. 331-344
    • Kunishima, N.1    Fukuyama, K.2    Matsubara, H.3    Hatanaka, H.4    Shibano, Y.5    Amachi, T.6
  • 55
    • 0037388770 scopus 로고    scopus 로고
    • Crystal structure of the ascorbate peroxidase-ascorbate complex
    • Sharp, K. H., Mewies, M., Moody, P. C., and Raven, E. I. (2003) Crystal structure of the ascorbate peroxidase-ascorbate complex Nat. Struct. Biol. 10, 303-307
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 303-307
    • Sharp, K.H.1    Mewies, M.2    Moody, P.C.3    Raven, E.I.4
  • 58
    • 74049108181 scopus 로고    scopus 로고
    • Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases. Binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7 Å resolution
    • Singh, A. K., Kumar, R. P., Pandey, N., Singh, N., Sinha, M., Ghushan, A., Kaur, P., Sharma, S., and Singh, T. P. (2010) Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases. Binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7 Å resolution J. Biol. Chem. 285, 1569-1576
    • (2010) J. Biol. Chem. , vol.285 , pp. 1569-1576
    • Singh, A.K.1    Kumar, R.P.2    Pandey, N.3    Singh, N.4    Sinha, M.5    Ghushan, A.6    Kaur, P.7    Sharma, S.8    Singh, T.P.9
  • 61
    • 1642527100 scopus 로고    scopus 로고
    • Structural, NMR and EPR studies of S = 1/2 and S = 3/2 Fe(III) bis-4-cyanopyridine complexes with dodecasubstituted porphyrins
    • Yatsunyk, L. A. and Walker, F. A. (2004) Structural, NMR and EPR studies of S = 1/2 and S = 3/2 Fe(III) bis-4-cyanopyridine complexes with dodecasubstituted porphyrins Inorg. Chem. 43, 757-777
    • (2004) Inorg. Chem. , vol.43 , pp. 757-777
    • Yatsunyk, L.A.1    Walker, F.A.2
  • 62
    • 3142708719 scopus 로고    scopus 로고
    • 1 ground state Fe(III) bis-(tert -butylisocyanide) complexes of dodecasubstituted porphyrinates
    • 1 ground state Fe(III) bis-(tert -butylisocyanide) complexes of dodecasubstituted porphyrinates Inorg. Chem. 43, 4341-4352
    • (2004) Inorg. Chem. , vol.43 , pp. 4341-4352
    • Yatsunyk, L.A.1    Walker, F.A.2
  • 63
    • 15944402770 scopus 로고    scopus 로고
    • NMR and EPR studies of the bis-pyridine and bis- t -butylisocyanide complexes of iron(III) octaethylchlorin
    • Cai, S., Lichtenberger, D. L., and Walker, F. A. (2005) NMR and EPR studies of the bis-pyridine and bis- t -butylisocyanide complexes of iron(III) octaethylchlorin Inorg. Chem. 44, 1890-1903
    • (2005) Inorg. Chem. , vol.44 , pp. 1890-1903
    • Cai, S.1    Lichtenberger, D.L.2    Walker, F.A.3
  • 64
    • 33646415091 scopus 로고    scopus 로고
    • NMR and EPR studies of chloroiron(III) tetraphenylchlorin and its complexes with imidazoles and pyridines of widely differing basicities
    • Cai, S., Shokhireva, T. K., Lichtenberger, D. L., and Walker, F. A. (2006) NMR and EPR studies of chloroiron(III) tetraphenylchlorin and its complexes with imidazoles and pyridines of widely differing basicities Inorg. Chem. 45, 3519-3531
    • (2006) Inorg. Chem. , vol.45 , pp. 3519-3531
    • Cai, S.1    Shokhireva, T.K.2    Lichtenberger, D.L.3    Walker, F.A.4
  • 67
    • 0035849509 scopus 로고    scopus 로고
    • Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes
    • Ivancich, A., Mazza, G., and Desbois, A. (2001) Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes Biochemistry 40, 6860-6866
    • (2001) Biochemistry , vol.40 , pp. 6860-6866
    • Ivancich, A.1    Mazza, G.2    Desbois, A.3
  • 68
    • 12044259988 scopus 로고
    • Models of the cytochromes b. Control of axial ligand orientation with a 'hindered' porphyrin system
    • Safo, M. K., Gupta, G. P., Walker, F. A., and Scheidt, W. R. (1991) Models of the cytochromes b. Control of axial ligand orientation with a 'hindered' porphyrin system J. Am. Chem. Soc. 113, 5497-5510
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5497-5510
    • Safo, M.K.1    Gupta, G.P.2    Walker, F.A.3    Scheidt, W.R.4
  • 69
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme-containing oxygenases and peroxidases
    • Dawson, J. H. (1988) Probing structure-function relations in heme-containing oxygenases and peroxidases Science 240, 433-439
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 70
    • 0023810222 scopus 로고
    • Heme enzyme crystal structures
    • Poulos, T. L. (1987) Heme enzyme crystal structures Adv. Inorg. Biochem. 7, 1-36
    • (1987) Adv. Inorg. Biochem. , vol.7 , pp. 1-36
    • Poulos, T.L.1
  • 71
    • 0002435698 scopus 로고    scopus 로고
    • Peroxidase and Cytochrome P450 Structures
    • In (, Eds.) Vol., pp - 218, Academic Press, San Diego.
    • Poulos, T. L. (2000) Peroxidase and Cytochrome P450 Structures. In The Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 4, pp 189 - 218, Academic Press, San Diego.
    • (2000) The Porphyrin Handbook , vol.4 , pp. 189
    • Poulos, T.L.1    Kadish, K.M.2    Smith, K.M.3    Guilard, R.4
  • 72
    • 77954267927 scopus 로고    scopus 로고
    • Thirty years of heme peroxidase structural biology
    • Poulos, T. L. (2010) Thirty years of heme peroxidase structural biology Arch. Biochem. Biophys. 500, 3-12
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 3-12
    • Poulos, T.L.1


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