메뉴 건너뛰기




Volumn 46, Issue 18, 2007, Pages 5323-5329

High-stability semiquinone intermediate in nitrate reductase a (NarGHI) from Escherichia coli is located in a quinol oxidation site close to Heme b D

Author keywords

[No Author keywords available]

Indexed keywords

DENITRIFICATION; ESCHERICHIA COLI; MUTAGENESIS; NITRATES; OXIDATION; REACTION KINETICS;

EID: 34248224968     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700074y     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0037716159 scopus 로고    scopus 로고
    • Protonmotive force generation by a redox loop mechanism
    • Jormakka, M., Byrne, B., and Iwata, S. (2003) Protonmotive force generation by a redox loop mechanism, FEBS Lett. 545, 25-30.
    • (2003) FEBS Lett , vol.545 , pp. 25-30
    • Jormakka, M.1    Byrne, B.2    Iwata, S.3
  • 3
    • 0035102909 scopus 로고    scopus 로고
    • The coordination and function of the redox centres of the membrane-bound nitrate reductases
    • Blasco, F., Guigliarelli, B., Magalon, A., Asso, M., Giordano, G., and Rothery, R. A. (2001) The coordination and function of the redox centres of the membrane-bound nitrate reductases, Cell. Mol. Life Sci. 58, 179-193.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 179-193
    • Blasco, F.1    Guigliarelli, B.2    Magalon, A.3    Asso, M.4    Giordano, G.5    Rothery, R.A.6
  • 4
    • 0035088582 scopus 로고    scopus 로고
    • The diheme cytochrome b subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI): Structure, function, and interaction with quinols
    • Rothery, R. A., Blasco, F., Magalon, A., and Weiner, J. H. (2001) The diheme cytochrome b subunit (NarI) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols, J. Mol. Microbiol. Biotechnol. 3, 273-283.
    • (2001) J. Mol. Microbiol. Biotechnol , vol.3 , pp. 273-283
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Weiner, J.H.4
  • 5
    • 13444257422 scopus 로고    scopus 로고
    • Evidence for an EPR-detectable semiquinone intermediate stabilized in the membrane-bound subunit NarI of nitrate reductase A (NarGHI) from Escherichia coli
    • Grimaldi, S., Lanciano, P., Bertrand, P., Blasco, F., and Guigliarelli, B. (2005) Evidence for an EPR-detectable semiquinone intermediate stabilized in the membrane-bound subunit NarI of nitrate reductase A (NarGHI) from Escherichia coli, Biochemistry 44, 1300-1308.
    • (2005) Biochemistry , vol.44 , pp. 1300-1308
    • Grimaldi, S.1    Lanciano, P.2    Bertrand, P.3    Blasco, F.4    Guigliarelli, B.5
  • 8
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems I and II
    • Nelson, N., and Yocum, C. F. (2006) Structure and function of photosystems I and II, Annu. Rev. Plant Biol. 57, 521-565.
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 9
    • 17644373498 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A
    • Bertero, M. G., Rothery, R. A., Boroumand, N., Palak, M., Blasco, F., Ginet, N., Weiner, J. H., and Strynadka, N. C. (2005) Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A, J. Biol. Chem. 280, 14836-14843.
    • (2005) J. Biol. Chem , vol.280 , pp. 14836-14843
    • Bertero, M.G.1    Rothery, R.A.2    Boroumand, N.3    Palak, M.4    Blasco, F.5    Ginet, N.6    Weiner, J.H.7    Strynadka, N.C.8
  • 10
    • 0344198175 scopus 로고    scopus 로고
    • Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: A stopped-flow study
    • Zhao, Z., Rothery, R. A., and Weiner, J. H. (2003) Effects of site-directed mutations on heme reduction in Escherichia coli nitrate reductase A by menaquinol: a stopped-flow study, Biochemistry 42, 14225-14233.
    • (2003) Biochemistry , vol.42 , pp. 14225-14233
    • Zhao, Z.1    Rothery, R.A.2    Weiner, J.H.3
  • 11
    • 0031306837 scopus 로고    scopus 로고
    • Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors - different reaction sites for menadiol and duroquinol
    • Giordani, R., Buc, J., Cornish-Bowden, A., and Cardenas, M. L. (1997) Kinetics of membrane-bound nitrate reductase A from Escherichia coli with analogues of physiological electron donors - different reaction sites for menadiol and duroquinol, Eur. J. Biochem. 250, 567-577.
    • (1997) Eur. J. Biochem , vol.250 , pp. 567-577
    • Giordani, R.1    Buc, J.2    Cornish-Bowden, A.3    Cardenas, M.L.4
  • 12
    • 3042565153 scopus 로고    scopus 로고
    • Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli
    • Giordani, R., and Buc, J. (2004) Evidence for two different electron transfer pathways in the same enzyme, nitrate reductase A from Escherichia coli, Eur. J. Biochem. 271, 2400-2407.
    • (2004) Eur. J. Biochem , vol.271 , pp. 2400-2407
    • Giordani, R.1    Buc, J.2
  • 13
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters
    • Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G., and Blasco, F. (1996) Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters, Biochemistry 35, 4828-4836.
    • (1996) Biochemistry , vol.35 , pp. 4828-4836
    • Guigliarelli, B.1    Magalon, A.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Blasco, F.7
  • 14
    • 0030845184 scopus 로고    scopus 로고
    • Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A
    • Magalon, A., Lemesle-Meunier, D., Rothery, R. A., Frixon, C., Weiner, J. H., and Blasco, F. (1997) Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A, J. Biol. Chem. 272, 25652-25658.
    • (1997) J. Biol. Chem , vol.272 , pp. 25652-25658
    • Magalon, A.1    Lemesle-Meunier, D.2    Rothery, R.A.3    Frixon, C.4    Weiner, J.H.5    Blasco, F.6
  • 15
    • 0035341125 scopus 로고    scopus 로고
    • L to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI)
    • L to the [3Fe-4S] cluster of Escherichia coli nitrate reductase A (NarGHI), Biochemistry 40, 5260-5268.
    • (2001) Biochemistry , vol.40 , pp. 5260-5268
    • Rothery, R.A.1    Blasco, F.2    Weiner, J.H.3
  • 16
    • 0026009206 scopus 로고
    • Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis
    • Rothery, R. A., and Weiner, J. H. (1991) Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis, Biochemistry 30, 8296-8305.
    • (1991) Biochemistry , vol.30 , pp. 8296-8305
    • Rothery, R.A.1    Weiner, J.H.2
  • 17
    • 0033613194 scopus 로고    scopus 로고
    • The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to narI
    • Rothery, R. A., Blasco, F., Magalon, A., Asso, M., and Weiner, J. H. (1999) The hemes of Escherichia coli nitrate reductase A (NarGHI): potentiometric effects of inhibitor binding to narI, Biochemistry 38, 12747-12757.
    • (1999) Biochemistry , vol.38 , pp. 12747-12757
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Asso, M.4    Weiner, J.H.5
  • 19
    • 0027406134 scopus 로고
    • Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes
    • Augier, V., Guigliarelli, B., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Chippaux, M., and Blasco, F. (1993) Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes, Biochemistry 32, 2013-2023.
    • (1993) Biochemistry , vol.32 , pp. 2013-2023
    • Augier, V.1    Guigliarelli, B.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Chippaux, M.7    Blasco, F.8
  • 20
    • 0022821997 scopus 로고
    • Reconstitution of a functional electron-transfer chain from purified formate dehydrogenase and fumarate reductase complexes
    • Unden, G., and Kroger, A. (1986) Reconstitution of a functional electron-transfer chain from purified formate dehydrogenase and fumarate reductase complexes, Methods Enzymol. 126, 387-399.
    • (1986) Methods Enzymol , vol.126 , pp. 387-399
    • Unden, G.1    Kroger, A.2
  • 21
    • 0038627545 scopus 로고    scopus 로고
    • Multifrequency cw-EPR investigation of the catalytic molybdenum cofactor of polysulfide reductase from Wolinella succinogenes
    • Prisner, T., Lyubenova, S., Atabay, Y., MacMillan, F., Kroger, A., and Klimmek, O. (2003) Multifrequency cw-EPR investigation of the catalytic molybdenum cofactor of polysulfide reductase from Wolinella succinogenes, J. Biol. Inorg. Chem. 8, 419-426.
    • (2003) J. Biol. Inorg. Chem , vol.8 , pp. 419-426
    • Prisner, T.1    Lyubenova, S.2    Atabay, Y.3    MacMillan, F.4    Kroger, A.5    Klimmek, O.6
  • 24
  • 29
    • 0022005264 scopus 로고
    • Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroides
    • Lubitz, W., Abresch, E. C., Debus, R. J., Isaacson, R. A., Okamura, M. Y., and Feher, G. (1985) Electron nuclear double resonance of semiquinones in reaction centers of Rhodopseudomonas sphaeroides, Biochim. Biophys. Acta 808, 464-469.
    • (1985) Biochim. Biophys. Acta , vol.808 , pp. 464-469
    • Lubitz, W.1    Abresch, E.C.2    Debus, R.J.3    Isaacson, R.A.4    Okamura, M.Y.5    Feher, G.6
  • 31
    • 0034598939 scopus 로고    scopus 로고
    • A motif for quinone binding sites in respiratory and photosynthetic systems
    • Fisher, N., and Rich, P. R. (2000) A motif for quinone binding sites in respiratory and photosynthetic systems, J. Mol. Biol. 296, 1153-1162.
    • (2000) J. Mol. Biol , vol.296 , pp. 1153-1162
    • Fisher, N.1    Rich, P.R.2
  • 32
    • 0032127499 scopus 로고    scopus 로고
    • Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli
    • Hastings, S. F., Kaysser, T. M., Jiang, F., Salerno, J. C., Gennis, R. B., and Ingledew, W. J. (1998) Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli, Eur. J. Biochem. 255, 317-323.
    • (1998) Eur. J. Biochem , vol.255 , pp. 317-323
    • Hastings, S.F.1    Kaysser, T.M.2    Jiang, F.3    Salerno, J.C.4    Gennis, R.B.5    Ingledew, W.J.6
  • 33
    • 33748750538 scopus 로고    scopus 로고
    • Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli
    • Maklashina, E., Hellwig, P., Rothery, R. A., Kotlyar, V., Sher, Y., Weiner, J. H., and Cecchini, G. (2006) Differences in protonation of ubiquinone and menaquinone in fumarate reductase from Escherichia coli, J. Biol. Chem. 281, 26655-26664.
    • (2006) J. Biol. Chem , vol.281 , pp. 26655-26664
    • Maklashina, E.1    Hellwig, P.2    Rothery, R.A.3    Kotlyar, V.4    Sher, Y.5    Weiner, J.H.6    Cecchini, G.7
  • 34
    • 2542510506 scopus 로고    scopus 로고
    • An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site
    • Hagerhall, C., Magnitsky, S., Sled, V. D., Schroder, I., Gunsalus, R. P., Cecchini, G., and Ohnishi, T. (1999) An Escherichia coli mutant quinol:fumarate reductase contains an EPR-detectable semiquinone stabilized at the proximal quinone-binding site, J. Biol. Chem. 274, 26157-26164.
    • (1999) J. Biol. Chem , vol.274 , pp. 26157-26164
    • Hagerhall, C.1    Magnitsky, S.2    Sled, V.D.3    Schroder, I.4    Gunsalus, R.P.5    Cecchini, G.6    Ohnishi, T.7
  • 35
    • 0037013281 scopus 로고    scopus 로고
    • Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site
    • Iverson, T. M., Luna-Chavez, C., Croal, L. R., Cecchini, G., and Rees, D. C. (2002) Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site, J. Biol. Chem. 277, 16124-16130.
    • (2002) J. Biol. Chem , vol.277 , pp. 16124-16130
    • Iverson, T.M.1    Luna-Chavez, C.2    Croal, L.R.3    Cecchini, G.4    Rees, D.C.5
  • 37
    • 33845697320 scopus 로고    scopus 로고
    • X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination
    • Rodrigues, M. L., Oliveira, T. F., Pereira, I. A., and Archer, M. (2006) X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination, EMBO J. 25, 5951-5960.
    • (2006) EMBO J , vol.25 , pp. 5951-5960
    • Rodrigues, M.L.1    Oliveira, T.F.2    Pereira, I.A.3    Archer, M.4
  • 39
    • 33846430018 scopus 로고    scopus 로고
    • Protein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: II. Geometry of the hydrogen bonds to the primary quinone formula by 1H and 2H ENDOR spectroscopy
    • Flores, M., Isaacson, R., Abresch, E., Calvo, R., Lubitz, W., and Feher, G. (2007) Protein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: II. Geometry of the hydrogen bonds to the primary quinone formula by 1H and 2H ENDOR spectroscopy, Biophys. J. 92, 671-682.
    • (2007) Biophys. J , vol.92 , pp. 671-682
    • Flores, M.1    Isaacson, R.2    Abresch, E.3    Calvo, R.4    Lubitz, W.5    Feher, G.6
  • 40
    • 0038558153 scopus 로고    scopus 로고
    • Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol
    • Zhao, Z., Rothery, R. A., and Weiner, J. H. (2003) Transient kinetic studies of heme reduction in Escherichia coli nitrate reductase A (NarGHI) by menaquinol, Biochemistry 42, 5403-5413.
    • (2003) Biochemistry , vol.42 , pp. 5403-5413
    • Zhao, Z.1    Rothery, R.A.2    Weiner, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.