메뉴 건너뛰기




Volumn 44, Issue 22, 2005, Pages 8068-8077

Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; ELECTRON TRANSITIONS; ESCHERICHIA COLI; IRON; PARAMAGNETIC RESONANCE; PROTEINS; SILICA; SOLVENTS; SULFUR;

EID: 20144366138     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050362p     Document Type: Article
Times cited : (21)

References (66)
  • 1
    • 0021847848 scopus 로고
    • Dimethyl sulfoxide reductase activity by anaerobically grown Escherichia coli HB101
    • Bilous, P. T., and Weiner, J. H. (1985) Dimethyl sulfoxide reductase activity by anaerobically grown Escherichia coli HB101, J. Bacteriol. 162, 1151-1155.
    • (1985) J. Bacteriol. , vol.162 , pp. 1151-1155
    • Bilous, P.T.1    Weiner, J.H.2
  • 2
    • 0025002494 scopus 로고
    • Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli
    • Sambasivarao, D., Scraba, D. O., Trieber, C., and Weiner, J. H. (1990) Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli, J. Bacteriol. 172, 5938-5948.
    • (1990) J. Bacteriol. , vol.172 , pp. 5938-5948
    • Sambasivarao, D.1    Scraba, D.O.2    Trieber, C.3    Weiner, J.H.4
  • 3
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • Bilous, P. T., Cole, S. T., Anderson, W. F., and Weiner, J. H. (1988) Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2, 785-795.
    • (1988) Mol. Microbiol. , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 4
    • 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
  • 5
    • 0029854878 scopus 로고    scopus 로고
    • Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
    • Simala-Orant, J. L., and Weiner, J. H. (1996) Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase, Microbiology 142 (Part 11), 3231-3239.
    • (1996) Microbiology , vol.142 , Issue.PART 11 , pp. 3231-3239
    • Simala-Orant, J.L.1    Weiner, J.H.2
  • 6
    • 0026800924 scopus 로고
    • Molecular analysis of dimethylsulfoxide reductase: A complex iron-sulfur molybdoenzyme of Escherichia coli
    • Weiner, J. H., Rothery, R. A., Sambasivarao, D., and Trieber, C. A. (1992) Molecular analysis of dimethylsulfoxide reductase: A complex iron-sulfur molybdoenzyme of Escherichia coli, Biochim. Biophys. Acta 1102, 1-18.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 1-18
    • Weiner, J.H.1    Rothery, R.A.2    Sambasivarao, D.3    Trieber, C.A.4
  • 7
    • 0034698130 scopus 로고    scopus 로고
    • Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli
    • Sambasivarao, D., Turner, R. J., Simala-Orant, J. L., Shaw, G., Hu, J., and Weiner, J. H. (2000) Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide reductase of Escherichia coli, J. Biol. Chem. 275, 22526-22531.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22526-22531
    • Sambasivarao, D.1    Turner, R.J.2    Simala-Orant, J.L.3    Shaw, G.4    Hu, J.5    Weiner, J.H.6
  • 8
    • 0028936979 scopus 로고
    • Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: Effect of tungstate and a mob mutation
    • Rothery, R. A., Grant, J. L., Johnson, J. L., Rajagopalan, K. V., and Weiner, J. H. (1995) Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: Effect of tungstate and a mob mutation, J. Bacteriol. 177, 2057-2063.
    • (1995) J. Bacteriol. , vol.177 , pp. 2057-2063
    • Rothery, R.A.1    Grant, J.L.2    Johnson, J.L.3    Rajagopalan, K.V.4    Weiner, J.H.5
  • 9
    • 0025088388 scopus 로고
    • Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli
    • Cammack, R., and Weiner, J. H. (1990) Electron paramagnetic resonance spectroscopic characterization of dimethyl sulfoxide reductase of Escherichia coli, Biochemistry 29, 8410-8416.
    • (1990) Biochemistry , vol.29 , pp. 8410-8416
    • Cammack, R.1    Weiner, J.H.2
  • 10
    • 0027460079 scopus 로고
    • The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli
    • Weiner, J. H., Shaw, G., Turner, R. J., and Trieber, C. A. (1993) The topology of the anchor subunit of dimethyl sulfoxide reductase of Escherichia coli, J. Biol. Chem. 268, 3238-3244.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3238-3244
    • Weiner, J.H.1    Shaw, G.2    Turner, R.J.3    Trieber, C.A.4
  • 11
    • 0026075272 scopus 로고
    • Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
    • Sambasivarao, D., and Weiner, J. H. (1991) Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation, J. Bacteriol. 173, 5935-5943.
    • (1991) J. Bacteriol. , vol.173 , pp. 5935-5943
    • Sambasivarao, D.1    Weiner, J.H.2
  • 12
    • 0029881885 scopus 로고    scopus 로고
    • Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase
    • Rothery, R. A., and Weiner, J. H. (1996) Interaction of an engineered [3Fe-4S] cluster with a menaquinol binding site of Escherichia coli DMSO reductase, Biochemistry 35, 3247-3257.
    • (1996) Biochemistry , vol.35 , pp. 3247-3257
    • Rothery, R.A.1    Weiner, J.H.2
  • 13
    • 1642575113 scopus 로고    scopus 로고
    • Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli
    • Geijer, P., and Weiner, J. H. (2004) Glutamate 87 is important for menaquinol binding in DmsC of the DMSO reductase (DmsABC) from Escherichia coli, Biochim. Biophys. Acta 1660, 66-74.
    • (2004) Biochim. Biophys. Acta , vol.1660 , pp. 66-74
    • Geijer, P.1    Weiner, J.H.2
  • 14
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka, M., Tornroth, S., Byrne, B., and Iwata, S. (2002) Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N, Science 295, 1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 15
    • 0025788382 scopus 로고
    • Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine
    • Berg, B. L., Li, J., Heider, J., and Stewart, V. (1991) Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine, J. Biol. Chem. 266, 22380-22385.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22380-22385
    • Berg, B.L.1    Li, J.2    Heider, J.3    Stewart, V.4
  • 16
    • 0028860781 scopus 로고
    • Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase
    • Abaibou, H., Pommier, J., Benoit, S., Giordano, G., and Mandrand-Berthelot, M. A. (1995) Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase, J. Bacteriol. 177, 7141-7149.
    • (1995) J. Bacteriol. , vol.177 , pp. 7141-7149
    • Abaibou, H.1    Pommier, J.2    Benoit, S.3    Giordano, G.4    Mandrand-Berthelot, M.A.5
  • 18
  • 19
    • 2442546646 scopus 로고    scopus 로고
    • The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state
    • Rothery, R. A., Bertero, M. G., Cammack, R., Palak, M., Blasco, F., Strynadka, N. C., and Weiner, J. H. (2004) The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state. Biochemistry 43, 5324-5333.
    • (2004) Biochemistry , vol.43 , pp. 5324-5333
    • Rothery, R.A.1    Bertero, M.G.2    Cammack, R.3    Palak, M.4    Blasco, F.5    Strynadka, N.C.6    Weiner, J.H.7
  • 20
    • 0029078973 scopus 로고
    • Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism
    • Heinzinger, N. K., Fujimoto, S. Y., Clark, M. A., Moreno, M. S., and Barrett, E. L. (1995) Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism. J. Bacteriol. 177, 2813-2820.
    • (1995) J. Bacteriol. , vol.177 , pp. 2813-2820
    • Heinzinger, N.K.1    Fujimoto, S.Y.2    Clark, M.A.3    Moreno, M.S.4    Barrett, E.L.5
  • 21
    • 0026550359 scopus 로고
    • Cloning and nucleotide sequence of the psrA gene of Wolinella sitccinogenes polysulphide reductase
    • Krafft, T., Bokranz, M., Klimmek, O., Schroder, I., Fahrenholz, F., Kojro, E., and Kroger, A. (1992) Cloning and nucleotide sequence of the psrA gene of Wolinella sitccinogenes polysulphide reductase, Eur. J. Biochem, 206, 503-510.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 503-510
    • Krafft, T.1    Bokranz, M.2    Klimmek, O.3    Schroder, I.4    Fahrenholz, F.5    Kojro, E.6    Kroger, A.7
  • 22
    • 0036179831 scopus 로고    scopus 로고
    • The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes
    • Dietrich, W., and Klimmek, O. (2002) The function of methyl-menaquinone-6 and polysulfide reductase membrane anchor (PsrC) in polysulfide respiration of Wolinella succinogenes. Eur. J. Biochem. 269, 1086-1095.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1086-1095
    • Dietrich, W.1    Klimmek, O.2
  • 23
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the β 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., Oiordano, G., and Blasco, F. (1996) Complete coordination of the four Fe-S centers of the β 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    Oiordano, G.6    Blasco, F.7
  • 24
    • 0032571394 scopus 로고    scopus 로고
    • The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters
    • Rothery, R. A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., and Weiner. J. H. (1998) The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). Effect of a mobAB mutation and interactions with [Fe-S] clusters, J. Biol. Chem. 273, 7462-7469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7462-7469
    • Rothery, R.A.1    Magalon, A.2    Giordano, G.3    Guigliarelli, B.4    Blasco, F.5    Weiner, J.H.6
  • 25
    • 0026560383 scopus 로고
    • [3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis
    • Manodori, A., Cecchini, G., Schroder, I., Gunsalus, R. P., Werth, M. T., and Johnson, M. K. (1992) [3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis, Biochemistry 31, 2703-2712.
    • (1992) Biochemistry , vol.31 , pp. 2703-2712
    • Manodori, A.1    Cecchini, G.2    Schroder, I.3    Gunsalus, R.P.4    Werth, M.T.5    Johnson, M.K.6
  • 26
    • 0029151127 scopus 로고
    • Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase
    • Kowal, A. T., Werth, M. T., Manodon, A., Cecchini, G., Schroder, I., Gunsalus, R. P., and Johnson, M. K. (1995) Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase, Biochemistry 34, 12284-12293.
    • (1995) Biochemistry , vol.34 , pp. 12284-12293
    • Kowal, A.T.1    Werth, M.T.2    Manodon, A.3    Cecchini, G.4    Schroder, I.5    Gunsalus, R.P.6    Johnson, M.K.7
  • 27
    • 0022406371 scopus 로고
    • The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex
    • Condon, C., Cammack, R., Patil, D. S., and Owen, P. (1985) The succinate dehydrogenase of Escherichia coli. Immunochemical resolution and biophysical characterization of a 4-subunit enzyme complex, J. Biol. Chem. 260, 9427-9434.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9427-9434
    • Condon, C.1    Cammack, R.2    Patil, D.S.3    Owen, P.4
  • 28
    • 9944232588 scopus 로고    scopus 로고
    • Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow
    • Unciuleac, M., Warkentin, E., Page, C. C., Boll, M., and Ermler, U. (2004) Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow. Structure 12, 2249-2256.
    • (2004) Structure , vol.12 , pp. 2249-2256
    • Unciuleac, M.1    Warkentin, E.2    Page, C.C.3    Boll, M.4    Ermler, U.5
  • 29
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction, Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 30
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page, C. C., Moser, C. C., and Dutton, P. L. (2003) Mechanism for electron transfer within and between proteins, Curr. Opin. Chem. Biol. 7, 551-556.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 31
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • Stephens, P. J., Jollie, D. R., and Warshel, A. (1996) Protein Control of Redox Potentials of Iron-Sulfur Proteins, Chem. Rev. 96, 2491-2514.
    • (1996) Chem. Rev. , vol.96 , pp. 2491-2514
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 34
    • 0028023334 scopus 로고
    • Calculation of the redox potentials of iron-sulfur proteins: The 2-/3-couple of [Fe4S*4Cys4] clusters in Peptococcus aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein
    • Jensen, G. M., Warshel, A., and Stephens, P. J. (1994) Calculation of the redox potentials of iron-sulfur proteins: The 2-/3-couple of [Fe4S*4Cys4] clusters in Peptococcus aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein, Biochemistry 33, 10911-10924.
    • (1994) Biochemistry , vol.33 , pp. 10911-10924
    • Jensen, G.M.1    Warshel, A.2    Stephens, P.J.3
  • 35
    • 0001282755 scopus 로고
    • NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianuin rubredoxin, and Chromatium high potential iron protein
    • Adman, E., Watenpaugh, K. D., and Jensen, L. H. (1975) NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianuin rubredoxin, and Chromatium high potential iron protein, Proc. Natl. Acad. Sci. U.S.A. 72, 4854-4858.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 4854-4858
    • Adman, E.1    Watenpaugh, K.D.2    Jensen, L.H.3
  • 36
    • 0026739955 scopus 로고
    • Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution
    • Rayment, I., Wesenberg, G., Meyer, T. E., Cusanovich, M. A., and Holden, H. M. (1992) Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution. J. Mol. Biol. 228, 672-686.
    • (1992) J. Mol. Biol. , vol.228 , pp. 672-686
    • Rayment, I.1    Wesenberg, G.2    Meyer, T.E.3    Cusanovich, M.A.4    Holden, H.M.5
  • 37
    • 0001396506 scopus 로고    scopus 로고
    • Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein
    • Jang, S. B., Seefeldt, L. C., and Peters, J. W. (2000) Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein, Biochemistry 39, 641-648.
    • (2000) Biochemistry , vol.39 , pp. 641-648
    • Jang, S.B.1    Seefeldt, L.C.2    Peters, J.W.3
  • 38
    • 0032525923 scopus 로고    scopus 로고
    • Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase
    • Rothery, R. A., and Weiner, J. H. (1998) Interaction of a menaquinol binding site with the [3Fe-4S] cluster of Escherichia coli fumarate reductase, Eur. J. Biochem. 254, 588-595.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 588-595
    • Rothery, R.A.1    Weiner, J.H.2
  • 39
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • Iverson, T. M., Luna-Chavez, C., Cecchini, G., and Rees, D. C. (1999) Structure of the Escherichia coli fumarate reductase respiratory complex, Science 284, 1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 41
    • 0343052744 scopus 로고    scopus 로고
    • Succinateiquinone oxidoreductases. Variations on a conserved theme
    • Hagerhall, C. (1997) Succinateiquinone oxidoreductases. Variations on a conserved theme, Biochim. Biophys. Acta 1320, 107-141.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hagerhall, C.1
  • 43
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A., and Sali, A. (2003) Modeller: Generation and refinement of homology-based protein structure models, Methods Enzymol. 374, 461-491.
    • (2003) Methods Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 45
    • 0033532204 scopus 로고    scopus 로고
    • Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase
    • Rothery, R. A., Trieber, C. A., and Weiner, J. H. (1999) Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase, J. Biol. Chem. 274, 13002-13009.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13002-13009
    • Rothery, R.A.1    Trieber, C.A.2    Weiner, J.H.3
  • 47
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M. A., Haas, S. M., Bieber, L. L., and Tolbert, N. E. (1978) A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples, Anal. Biochem. 87, 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 48
    • 0032524892 scopus 로고    scopus 로고
    • Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases
    • Rothery, R. A., Chatterjee, I., Kiema, G., McDermott, M. T., and Weiner, J. H. (1998) Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases, Biochem. J. 332 (Part 1), 35-41.
    • (1998) Biochem. J. , vol.332 , Issue.PART 1 , pp. 35-41
    • Rothery, R.A.1    Chatterjee, I.2    Kiema, G.3    McDermott, M.T.4    Weiner, J.H.5
  • 49
    • 0017594519 scopus 로고
    • Binding of HQNO to beef-heart sub-mitochondrial particles
    • Van Ark, G., and Berden, J. A. (1977) Binding of HQNO to beef-heart sub-mitochondrial particles, Biochim. Biophys. Acta 459, 119-127.
    • (1977) Biochim. Biophys. Acta , vol.459 , pp. 119-127
    • Van Ark, G.1    Berden, J.A.2
  • 50
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase)
    • Okun, J. G., Lummen, P., and Brandt, U. (1999) Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase), J. Biol. Chem. 274, 2625-2630.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 51
    • 0032516875 scopus 로고    scopus 로고
    • Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli
    • Zhao, Z., and Weiner, J. H. (1998) Interaction of 2-n-heptyl-4- hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli, J. Biol. Chem. 273, 20758-20763.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20758-20763
    • Zhao, Z.1    Weiner, J.H.2
  • 52
    • 0028944291 scopus 로고
    • Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
    • Berks, B. C., Page, M. D., Richardson, D. J., Reilly, A., Cavill, A., Outen, F., and Ferguson, S. J. (1995) Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop, Mol. Microbiol. 15, 319-331.
    • (1995) Mol. Microbiol. , vol.15 , pp. 319-331
    • Berks, B.C.1    Page, M.D.2    Richardson, D.J.3    Reilly, A.4    Cavill, A.5    Outen, F.6    Ferguson, S.J.7
  • 53
    • 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
  • 55
    • 0034964421 scopus 로고    scopus 로고
    • Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma
    • Astuti, D., Latif, F., Dallol, A., Dahia, P. L., Douglas, F., George, E., Skoldberg, F., Husebye, E. S., Eng, C., and Maher, E. R. (2001) Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma, Am. J. Hum. Genet. 69, 49-54.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 49-54
    • Astuti, D.1    Latif, F.2    Dallol, A.3    Dahia, P.L.4    Douglas, F.5    George, E.6    Skoldberg, F.7    Husebye, E.S.8    Eng, C.9    Maher, E.R.10
  • 56
    • 0028973038 scopus 로고
    • Reaction of cytochrome bos with oxygen: Extra redox center(s) are present in the protein
    • Wang, J., Rumbley, J., Ching, Y. C., Takahashi, S., Gennis, R. B., and Rousseau, D. L. (1995) Reaction of cytochrome bos with oxygen: Extra redox center(s) are present in the protein, Biochemistry 34, 15504-15511.
    • (1995) Biochemistry , vol.34 , pp. 15504-15511
    • Wang, J.1    Rumbley, J.2    Ching, Y.C.3    Takahashi, S.4    Gennis, R.B.5    Rousseau, D.L.6
  • 57
    • 0036254366 scopus 로고    scopus 로고
    • 1 complex: Predicted conformational changes and inhibition of proton translocation
    • 1 complex: Predicted conformational changes and inhibition of proton translocation, J. Bioenerg. Biomembr. 34, 81-88.
    • (2002) J. Bioenerg. Biomembr. , vol.34 , pp. 81-88
    • Wang, Y.1    Beattie, D.S.2
  • 58
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier, C., Harrenga, A., Ermler, U., and Michel, H. (1997) Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment, Proc. Natl. Acad. Sci. U.S.A. 94, 10547-10553.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 60
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • Barry, B. A., and Babcock, G. T. (1987) Tyrosine radicals are involved in the photosynthetic oxygen-evolving system, Proc. Natl. Acad. Sci. U.S.A. 84, 7099-7103.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 62
    • 0029745151 scopus 로고    scopus 로고
    • Elucidating the mechanism of nucleotide-dependent changes in the redox potential of the [4Fe-4S] cluster in nitrogenase iron protein: The role of phenylalanine 135
    • Ryle, M. J., Lanzilotta, W. N., and Seefeldt, L. C. (1996) Elucidating the mechanism of nucleotide-dependent changes in the redox potential of the [4Fe-4S] cluster in nitrogenase iron protein: The role of phenylalanine 135, Biochemistry 35, 9424-9434.
    • (1996) Biochemistry , vol.35 , pp. 9424-9434
    • Ryle, M.J.1    Lanzilotta, W.N.2    Seefeldt, L.C.3
  • 63
    • 0028832648 scopus 로고
    • Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): Physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP
    • Agarwal, A., Li, D., and Cowan, J. A. (1995) Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): Physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP, Proc. Natl. Acad. Sci. U.S.A. 92, 9440-9444.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9440-9444
    • Agarwal, A.1    Li, D.2    Cowan, J.A.3
  • 64
    • 0028879888 scopus 로고
    • Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: Evidence for the existence of two groups
    • Heering, H. A., Bulsink, B. M., Hagen, W. R., and Meyer, T. E. (1995) Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: Evidence for the existence of two groups, Biochemistry 34, 14675-14686.
    • (1995) Biochemistry , vol.34 , pp. 14675-14686
    • Heering, H.A.1    Bulsink, B.M.2    Hagen, W.R.3    Meyer, T.E.4
  • 65
    • 0033200167 scopus 로고    scopus 로고
    • Amino acid sequences of two high-potential iron-sulfur proteins (HiPIPs) from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salinarum
    • Ambler, R. P., Daniel, M., Meyer, T. E., and Cusanovich, M. A. (1999) Amino acid sequences of two high-potential iron-sulfur proteins (HiPIPs) from the moderately halophilic purple phototrophic bacterium, Rhodospirillum salinarum, Arch. Biochem. Biophys. 369, 143-148.
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 143-148
    • Ambler, R.P.1    Daniel, M.2    Meyer, T.E.3    Cusanovich, M.A.4
  • 66
    • 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.