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Volumn 45, Issue 2, 2006, Pages 427-438

Geometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: Vibrational and ENDOR studies

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRONIC STRUCTURE; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GEOMETRY; IRON; ISOTOPES; MOLECULAR VIBRATIONS; RESONANCE; SPECTROSCOPIC ANALYSIS;

EID: 30744475232     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052034v     Document Type: Article
Times cited : (18)

References (57)
  • 2
    • 0036933848 scopus 로고    scopus 로고
    • What biological purpose is served by superoxide reductase?
    • Imlay, J. A. (2002) What biological purpose is served by superoxide reductase?, J. Biol. Inorg. Chem. 7, 659-663.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 659-663
    • Imlay, J.A.1
  • 3
    • 0036941823 scopus 로고    scopus 로고
    • Superoxide scavenging by neelaredoxin: Dismutation and reduction activities in anaerobes
    • Abreu, I. A., Xavier, A. V., LeGall, J., Cabelli, D. E., and Teixeira, M. (2002) Superoxide scavenging by neelaredoxin: dismutation and reduction activities in anaerobes, J. Biol. Inorg. Chem. 7, 668-674.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 668-674
    • Abreu, I.A.1    Xavier, A.V.2    Legall, J.3    Cabelli, D.E.4    Teixeira, M.5
  • 4
    • 12144289472 scopus 로고    scopus 로고
    • Discovery of superoxide reductase: An historical perspective
    • Nivière, V., and Fontecave, M. (2004) Discovery of superoxide reductase: an historical perspective, J. Biol. Inorg. Chem. 9, 119-123.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 119-123
    • Nivière, V.1    Fontecave, M.2
  • 5
    • 9444254650 scopus 로고    scopus 로고
    • Microbial detoxification of superoxide: The non-heme iron reductive paradigm for combating oxidative stress
    • Kurtz, D. M., Jr. (2004) Microbial detoxification of superoxide: The non-heme iron reductive paradigm for combating oxidative stress, Acc. Chem. Res. 37, 902-908.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 902-908
    • Kurtz Jr., D.M.1
  • 6
    • 0034646208 scopus 로고    scopus 로고
    • Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
    • Yeh, A. P., Hu, Y., Jenney, F. E., Adams, M. W. W., and Rees, D. C. (2000) Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states, Biochemistry 39, 2499-2508.
    • (2000) Biochemistry , vol.39 , pp. 2499-2508
    • Yeh, A.P.1    Hu, Y.2    Jenney, F.E.3    Adams, M.W.W.4    Rees, D.C.5
  • 8
    • 0034703748 scopus 로고    scopus 로고
    • Superoxide reactivity of rubredoxin oxidoreductase (desulfoferrodoxin) from Desulfovibrio vulgaris: A pulse radiolysis study
    • Coulter, E. D., Emerson, J. P., Kurtz, D. M., Jr., and Cabelli, D. E. (2000) Superoxide reactivity of rubredoxin oxidoreductase (desulfoferrodoxin) from Desulfovibrio vulgaris: A pulse radiolysis study, J. Am. Chem. Soc. 122, 11555-11556.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11555-11556
    • Coulter, E.D.1    Emerson, J.P.2    Kurtz Jr., D.M.3    Cabelli, D.E.4
  • 9
    • 0035914396 scopus 로고    scopus 로고
    • The mechanism of superoxide scavenging by Archaeoglobus fulgidus neelaredoxin
    • Abreu, I. A., Saraiva, L. M., Soares, C. M., Teixeira, M., and Cabelli, D. E. (2001) The mechanism of superoxide scavenging by Archaeoglobus fulgidus neelaredoxin, J. Biol. Chem. 276, 38995-39001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38995-39001
    • Abreu, I.A.1    Saraiva, L.M.2    Soares, C.M.3    Teixeira, M.4    Cabelli, D.E.5
  • 10
    • 0035942349 scopus 로고    scopus 로고
    • Superoxide reductase from Desulfoarculus baarsii: Mechanism and role of glutamate 47 and lysine 48 in catalysis
    • Lombard, M., Houée-Levin, C., Touati, D., Fontecave, M., and Nivière, V. (2001) Superoxide reductase from Desulfoarculus baarsii: Mechanism and role of glutamate 47 and lysine 48 in catalysis, Biochemistry 40, 5032-5040.
    • (2001) Biochemistry , vol.40 , pp. 5032-5040
    • Lombard, M.1    Houée-Levin, C.2    Touati, D.3    Fontecave, M.4    Nivière, V.5
  • 11
    • 0037006991 scopus 로고    scopus 로고
    • Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris
    • Emerson, J. P., Coulter, E. D., Cabelli, D. E., Phillips, R. S., and Kurtz, D. M., Jr. (2002) Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris, Biochemistry 41, 4348-4357.
    • (2002) Biochemistry , vol.41 , pp. 4348-4357
    • Emerson, J.P.1    Coulter, E.D.2    Cabelli, D.E.3    Phillips, R.S.4    Kurtz Jr., D.M.5
  • 12
    • 0037031253 scopus 로고    scopus 로고
    • Resonance Raman characterization of the mononuclear iron active-site vibrations and putative electron transport pathways in Pyrococcus furiosus superoxide reductase
    • Clay, M. D., Jenney, F. E., Jr., Noh, H. J., Hagedoorn, P. L., Adams, M. W. W., and Johnson, M. K. (2002) Resonance Raman characterization of the mononuclear iron active-site vibrations and putative electron transport pathways in Pyrococcus furiosus superoxide reductase, Biochemistry 41, 9833-9841.
    • (2002) Biochemistry , vol.41 , pp. 9833-9841
    • Clay, M.D.1    Jenney Jr., F.E.2    Noh, H.J.3    Hagedoorn, P.L.4    Adams, M.W.W.5    Johnson, M.K.6
  • 13
    • 0037072267 scopus 로고    scopus 로고
    • Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: An FTIR study
    • Berthomieu, C., Dupeyrat, F., Fontecave, M., Verméglio, A., and Nivière, V. (2002) Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: An FTIR study, Biochemistry 41, 10360-10368.
    • (2002) Biochemistry , vol.41 , pp. 10360-10368
    • Berthomieu, C.1    Dupeyrat, F.2    Fontecave, M.3    Verméglio, A.4    Nivière, V.5
  • 14
    • 1642494864 scopus 로고    scopus 로고
    • Superoxide reductase from Desulfoarculus baarsii: Identification of protonation steps in the enzymatic mechanism
    • Nivière, V., Asso, M., Weill, C. O., Lombard, M., Guigliarelli, B., Favaudon, V., and Houée-Levin, C. (2004) Superoxide reductase from Desulfoarculus baarsii: Identification of protonation steps in the enzymatic mechanism, Biochemistry 43, 808-818.
    • (2004) Biochemistry , vol.43 , pp. 808-818
    • Nivière, V.1    Asso, M.2    Weill, C.O.3    Lombard, M.4    Guigliarelli, B.5    Favaudon, V.6    Houée-Levin, C.7
  • 15
    • 0042155690 scopus 로고    scopus 로고
    • Spectroscopic characterization of the [Fe(His)4(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris
    • Clay, M. D., Emerson, J. P., Coulter, E. D., Kurtz, D. M., Jr., and Johnson, M. K. (2003) Spectroscopic characterization of the [Fe(His)4(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris, J. Biol. Inorg. Chem. 8, 671-682.
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 671-682
    • Clay, M.D.1    Emerson, J.P.2    Coulter, E.D.3    Kurtz Jr., D.M.4    Johnson, M.K.5
  • 17
    • 0037028549 scopus 로고    scopus 로고
    • Spectroscopic studies of Pyrococcus furiosus superoxide reductase: Implications for active-site structures and the catalytic mechanism
    • Clay, M. D., Jenney, F. E., Jr., Hagedoorn, P. L., George, G. N., Adams, M. W. W., and Johnson, M. K. (2002) Spectroscopic studies of Pyrococcus furiosus superoxide reductase: Implications for active-site structures and the catalytic mechanism, J. Am. Chem. Soc. 124, 788-805.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 788-805
    • Clay, M.D.1    Jenney Jr., F.E.2    Hagedoorn, P.L.3    George, G.N.4    Adams, M.W.W.5    Johnson, M.K.6
  • 18
    • 0037467749 scopus 로고    scopus 로고
    • Computational study of the non-heme iron active site in superoxide reductase and its reaction with superoxide
    • Silaghi-Dumitrescu, R., Silaghi-Dumitrescu, I., Coulter, E. D., and Kurtz, D. M., Jr. (2003) Computational study of the non-heme iron active site in superoxide reductase and its reaction with superoxide, Inorg. Chem. 42, 446-456.
    • (2003) Inorg. Chem. , vol.42 , pp. 446-456
    • Silaghi-Dumitrescu, R.1    Silaghi-Dumitrescu, I.2    Coulter, E.D.3    Kurtz Jr., D.M.4
  • 19
    • 0037042234 scopus 로고    scopus 로고
    • Identification of iron-(III) peroxo species in the active site of the superoxide reductase sor from Desulfoarculus baarsii
    • Mathé, C., Mattioli, T. A., Horner, O., Lombard, M., Latour, J.-M., Fontecave, M., and Nivière, V. (2002) Identification of iron-(III) peroxo species in the active site of the superoxide reductase sor from Desulfoarculus baarsii, J. Am. Chem. Soc. 124, 4966-4967.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4966-4967
    • Mathé, C.1    Mattioli, T.A.2    Horner, O.3    Lombard, M.4    Latour, J.-M.5    Fontecave, M.6    Nivière, V.7
  • 23
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, F. E., Verhagen, M. F. J. M., Cui, X., and Adams, M. W. W. (1999) Anaerobic microbes: Oxygen detoxification without superoxide dismutase, Science 286, 306-309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney, F.E.1    Verhagen, M.F.J.M.2    Cui, X.3    Adams, M.W.W.4
  • 25
    • 0024106826 scopus 로고
    • A simple anaerobic cell for low-temperature Raman spectroscopy
    • Drozdzewski, P. M., and Johnson, M. K. (1988) A simple anaerobic cell for low-temperature Raman spectroscopy, Appl. Spectrosc. 42, 1575-1577.
    • (1988) Appl. Spectrosc. , vol.42 , pp. 1575-1577
    • Drozdzewski, P.M.1    Johnson, M.K.2
  • 27
    • 0002649493 scopus 로고
    • Sensitivity enhancement in field modulated CW ENDOR via RF bandwidth broadening
    • Hoffman, B. M., DeRose, V. J., Ong, J.-L., and Davoust, C. E. (1994) Sensitivity enhancement in field modulated CW ENDOR via RF bandwidth broadening, J. Magn. Reson. 110, 52-57.
    • (1994) J. Magn. Reson. , vol.110 , pp. 52-57
    • Hoffman, B.M.1    Derose, V.J.2    Ong, J.-L.3    Davoust, C.E.4
  • 29
    • 0028279008 scopus 로고
    • Resonance Raman study of cyanide-ligated horseradish peroxidase. Detection of two binding geometries and direct evidence for the "push-pull" effect
    • Al-Mustafa, J., and Kincaid, J. R. (1994) Resonance Raman study of cyanide-ligated horseradish peroxidase. Detection of two binding geometries and direct evidence for the "push-pull" effect, Biochemistry 33, 2191-2197.
    • (1994) Biochemistry , vol.33 , pp. 2191-2197
    • Al-Mustafa, J.1    Kincaid, J.R.2
  • 30
    • 0000301740 scopus 로고
    • Resonance Raman spectroscopic detection of both linear and bent Fe-CN fragments for the cyanide adducts of cytochrome P-450 camphor and its substrate-bound forms. Relevance to the "charge relay" mechanism
    • Simianu, M. C., and Kincaid, J. R. (1995) Resonance Raman spectroscopic detection of both linear and bent Fe-CN fragments for the cyanide adducts of cytochrome P-450 camphor and its substrate-bound forms. Relevance to the "charge relay" mechanism, J. Am. Chem. Soc. 117, 4628-4636.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4628-4636
    • Simianu, M.C.1    Kincaid, J.R.2
  • 31
    • 0027501847 scopus 로고
    • Distinctive heme active-site structure in lactoperoxidase revealed by resonance Raman spectroscopy
    • Hu, S., Treat, R. W., and Kincaid, J. R. (1993) Distinctive heme active-site structure in lactoperoxidase revealed by resonance Raman spectroscopy, Biochemistry 32, 10125-10130.
    • (1993) Biochemistry , vol.32 , pp. 10125-10130
    • Hu, S.1    Treat, R.W.2    Kincaid, J.R.3
  • 32
    • 0035900956 scopus 로고    scopus 로고
    • Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants
    • Deng, T.-J., Macdonald, I. D. G., Simianu, M. C., Sykora, M., Kincaid, J. R., and Sligar, S. G. (2001) Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants, J. Am. Chem. Soc. 123, 269-278.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 269-278
    • Deng, T.-J.1    Macdonald, I.D.G.2    Simianu, M.C.3    Sykora, M.4    Kincaid, J.R.5    Sligar, S.G.6
  • 33
    • 0028921266 scopus 로고
    • Resonance Raman investigation of cyanide ligated beef liver and Aspergillus niger catalases
    • Al-Mustafa, J., Sykora, M., and Kincaid, J. R. (1995) Resonance Raman investigation of cyanide ligated beef liver and Aspergillus niger catalases, J. Biol. Chem. 270, 10449-10460.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10449-10460
    • Al-Mustafa, J.1    Sykora, M.2    Kincaid, J.R.3
  • 34
    • 0025065381 scopus 로고
    • Metal-ligand vibrations of cyanoferric myeloperoxidase and cyanoferric horseradish peroxidase: Evidence for a constrained heme pocket in myeloperoxidase
    • López-Garriga, J. J., Oertling, W. A., Kean, R. T., Hoogland, H., Wever, R., and Babcock, G. T. (1990) Metal-ligand vibrations of cyanoferric myeloperoxidase and cyanoferric horseradish peroxidase: Evidence for a constrained heme pocket in myeloperoxidase, Biochemistry 29, 9387-9395.
    • (1990) Biochemistry , vol.29 , pp. 9387-9395
    • López-Garriga, J.J.1    Oertling, W.A.2    Kean, R.T.3    Hoogland, H.4    Wever, R.5    Babcock, G.T.6
  • 36
    • 1842513886 scopus 로고    scopus 로고
    • - adducts of hemoglobin, myoglobin, and cytochrome c oxidase: Evidence for vibrational coupling between the Fe-C-N bending and porphyrin in-plane modes
    • - adducts of hemoglobin, myoglobin, and cytochrome c oxidase: Evidence for vibrational coupling between the Fe-C-N bending and porphyrin in-plane modes, J. Phys. Chem. 100, 15274-15279.
    • (1996) J. Phys. Chem. , vol.100 , pp. 15274-15279
    • Hirota, S.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 37
    • 0024354883 scopus 로고
    • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes
    • Han, S., Madden, J. F., Siegel, L. M., and Spiro, T. G. (1989) Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes, Biochemistry 28, 5477-5485.
    • (1989) Biochemistry , vol.28 , pp. 5477-5485
    • Han, S.1    Madden, J.F.2    Siegel, L.M.3    Spiro, T.G.4
  • 38
    • 0035965691 scopus 로고    scopus 로고
    • Resonance Raman spectroscopic study of nitrophorin 1, a nitric oxide-binding heme protein from Rhodnius prolixus, and its nitrosyl and cyano adducts
    • Maes, E. M., Walker, F. A., Montfort, W. R., and Czernuszewicz, R. S. (2001) Resonance Raman spectroscopic study of nitrophorin 1, a nitric oxide-binding heme protein from Rhodnius prolixus, and its nitrosyl and cyano adducts, J. Am. Chem. Soc. 123, 11664-11672.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11664-11672
    • Maes, E.M.1    Walker, F.A.2    Montfort, W.R.3    Czernuszewicz, R.S.4
  • 39
    • 0021989717 scopus 로고
    • Investigations of cyanide as an infrared probe of hemoprotein ligand binding sites
    • Yoshikawa, S., O'Keeffe, D. H., and Caughey, W. S. (1985) Investigations of cyanide as an infrared probe of hemoprotein ligand binding sites, J. Biol. Chem. 260, 3518-3528.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3518-3528
    • Yoshikawa, S.1    O'Keeffe, D.H.2    Caughey, W.S.3
  • 44
    • 84950133864 scopus 로고    scopus 로고
    • Structural versatility of proteins containing rubredoxin-type centers
    • (Ferreira, G. C., Moura, J. J. G., and Franco, R., Eds.) Wiley-VCH Verlag, Weinheim
    • Romao, M. J., and Archer, M. (1999) Structural versatility of proteins containing rubredoxin-type centers, in Iron Metabolism (Ferreira, G. C., Moura, J. J. G., and Franco, R., Eds.) pp 341-358, Wiley-VCH Verlag, Weinheim.
    • (1999) Iron Metabolism , pp. 341-358
    • Romao, M.J.1    Archer, M.2
  • 45
    • 30744435257 scopus 로고
    • Electron magnetic resonance studies and covalent bonding of cyanide and fluoride complexes of transition metals
    • Kuska, H. A., and Rogers, M. T. (1964) Electron magnetic resonance studies and covalent bonding of cyanide and fluoride complexes of transition metals, J. Chem. Phys. 41, 3802-3805.
    • (1964) J. Chem. Phys. , vol.41 , pp. 3802-3805
    • Kuska, H.A.1    Rogers, M.T.2
  • 47
    • 0343616222 scopus 로고
    • Carbon-13 NMR of paramagnetic iron-group cyanides
    • Davis, D. G., and Kurland, R. J. (1967) Carbon-13 NMR of paramagnetic iron-group cyanides, J. Chem. Phys. 46, 388-390.
    • (1967) J. Chem. Phys. , vol.46 , pp. 388-390
    • Davis, D.G.1    Kurland, R.J.2
  • 48
    • 0001389357 scopus 로고
    • Electron nuclear double resonance from high- and low-spin ferric hemoglobins and myoglobins
    • Mulks, C. F., Scholes, C. P., Dickinson, L. C., and Lapidot, A. (1979) Electron nuclear double resonance from high- and low-spin ferric hemoglobins and myoglobins, J. Am. Chem. Soc. 101, 1645-1654.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 1645-1654
    • Mulks, C.F.1    Scholes, C.P.2    Dickinson, L.C.3    Lapidot, A.4
  • 50
    • 0004188383 scopus 로고
    • Oxford University Press, Oxford
    • McWeeny, R. (1979) Coulson's Valence, Oxford University Press, Oxford.
    • (1979) Coulson's Valence
    • McWeeny, R.1
  • 52
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: An X-ray crystallographic study
    • Bolognesi, M., Rosano, C., Losso, R., Borassi, A., Rizzi, M., Wittenberg, J. B., Boffi, A., and Ascenzi, P. (1999) Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-ray crystallographic study, Biophys. J. 77, 1093-1099.
    • (1999) Biophys. J. , vol.77 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5    Wittenberg, J.B.6    Boffi, A.7    Ascenzi, P.8
  • 53
    • 0035923432 scopus 로고    scopus 로고
    • Human myeloperoxidase: Structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution
    • Blair-Johnson, M., Fiedler, T., and Fenna, R. (2001) Human myeloperoxidase: Structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution, Biochemistry 40, 13990-13997.
    • (2001) Biochemistry , vol.40 , pp. 13990-13997
    • Blair-Johnson, M.1    Fiedler, T.2    Fenna, R.3
  • 56
    • 0029926452 scopus 로고    scopus 로고
    • Infrared spectroscopy of the cyanide complex of iron(II) myoglobin and comparison with complexes of microperoxidase and hemoglobin
    • Reddy, K. S., Yonetani, T., Tsuneshige, A., Chance, B., Kushkuley, B., Stavrov, S. S., and Vanderkooi, J. M. (1996) Infrared spectroscopy of the cyanide complex of iron(II) myoglobin and comparison with complexes of microperoxidase and hemoglobin, Biochemistry 35, 5562-5570.
    • (1996) Biochemistry , vol.35 , pp. 5562-5570
    • Reddy, K.S.1    Yonetani, T.2    Tsuneshige, A.3    Chance, B.4    Kushkuley, B.5    Stavrov, S.S.6    Vanderkooi, J.M.7
  • 57
    • 0035110522 scopus 로고    scopus 로고
    • Is the CO adduct of myoglobin bent, and does it matter?
    • Spiro, T. G., and Kozlowski, P. M. (2001) Is the CO adduct of myoglobin bent, and does it matter?, Acc. Chem. Res. 34, 137-144.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 137-144
    • Spiro, T.G.1    Kozlowski, P.M.2


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