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Volumn 50, Issue 20, 2011, Pages 4263-4272

Zinc inhibition of bacterial cytochrome bc1 reveals the role of cytochrome b E295 in proton release at the Qo site

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; APPARENT K; BINDING AFFINITIES; BINDING MECHANISMS; COFACTORS; CYTOCHROME B; DIFFERENCE SPECTROSCOPY; EFFLUX PATHWAYS; ELECTRON TRANSFER; ELECTRON TRANSFERRING; EXTENDED X-RAY ABSORPTION FINE STRUCTURES; FOURIER TRANSFORM INFRARED; FTIR; HIGH-AFFINITY SITES; INHIBITORY EFFECT; ISOTHERMAL TITRATION CALORIMETRY; KINETIC ANALYSIS; KINETIC STUDY; MOLECULAR BASIS; PROTON RELEASE; PROTON-COUPLED ELECTRON TRANSFER; PROTON-MOTIVE FORCES; PROTONATED; REDOX POTENTIALS; RHODOBACTER CAPSULATUS; WILD TYPES;

EID: 79956208939     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200230e     Document Type: Article
Times cited : (29)

References (50)
  • 1
    • 33745622830 scopus 로고    scopus 로고
    • Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain
    • DOI 10.1016/j.bbabio.2006.03.015, PII S0005272806000703
    • Papa, S., Lorusso, M., and Di Paola, M. (2006) Cooperativity and flexibility of the protonmotive activity of mitochondrial respiratory chain Biochim. Biophys. Acta 1757, 428-436 (Pubitemid 43993851)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.5-6 , pp. 428-436
    • Papa, S.1    Lorusso, M.2    Di Paola, M.3
  • 9
    • 0029670892 scopus 로고    scopus 로고
    • y of Rhodobacter capsulatus can serve as an electron donor to the photosynthetic reaction of Rhodobacter sphaeroides
    • y of Rhodobacter capsulatus can serve as an electron donor to the photosynthetic reaction of Rhodobacter sphaeroides Biochim. Biophys. Acta 1273, 159-164
    • (1996) Biochim. Biophys. Acta , vol.1273 , pp. 159-164
    • Jenney Jr., F.E.1    Prince, R.C.2    Daldal, F.3
  • 10
    • 0028231734 scopus 로고
    • 2 and membrane-associated cytochrome c(y) of Rhodobacter capsulatus in photosynthetic electron transfer
    • y of Rhodobacter capsulatus in photosynthetic electron transfer Biochemistry 33, 2496-2502 (Pubitemid 24099656)
    • (1994) Biochemistry , vol.33 , Issue.9 , pp. 2496-2502
    • Jenney Jr., F.E.1    Prince, R.C.2    Daldal, F.3
  • 11
    • 0027503597 scopus 로고
    • A novel membrane-associated c-type cytochrome, cyt c(y), can mediate the photosynthetic growth of Rhodobacter capsulatus and Rhodobacter sphaeroides
    • y, can mediate the photosynthetic growth of Rhodobacter capsulatus and Rhodobacter sphaeroides EMBO J. 12, 1283-1292 (Pubitemid 23112783)
    • (1993) EMBO Journal , vol.12 , Issue.4 , pp. 1283-1292
    • Jenney Jr., F.E.1    Daldal, F.2
  • 13
    • 0032522160 scopus 로고    scopus 로고
    • Dicyclohexylcarbodiimide inhibits proton pumping in ubiquinol: Cytochrome c oxidoreductase of rhodobacter sphaeroides and binds to aspartate-187 of cytochrome b
    • DOI 10.1006/abbi.1998.0590
    • Wang, Y., Obungu, V., and Beattie, D. S. (1998) Dicyclohexylcarbodiimide inhibits proton pumping in ubiquinol:cytochrome c oxidoreductase of Rhodobacter sphaeroides and binds to aspartate-187 of cytochrome b Arch. Biochem. Biophys. 352, 193-198 (Pubitemid 28368584)
    • (1998) Archives of Biochemistry and Biophysics , vol.352 , Issue.2 , pp. 193-198
    • Wang, Y.1    Obungu, V.2    Beattie, D.S.3
  • 14
    • 0034719107 scopus 로고    scopus 로고
    • DCCD inhibits the reactions of the iron-sulfur protein in Rhodobacter sphaeroides chromatophores
    • DOI 10.1021/bi001482u
    • Shinkarev, V. P., Ugulava, N. B., Crofts, A. R., and Wraight, C. A. (2000) DCCD inhibits the reactions of the iron-sulfur protein in Rhodobacter sphaeroides chromatophores Biochemistry 39, 16206-16212 (Pubitemid 32038284)
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 16206-16212
    • Shinkarev, V.P.1    Ugulava, N.B.2    Crofts, A.R.3    Wraight, C.A.4
  • 15
    • 0034700317 scopus 로고    scopus 로고
    • Aspartate-187 of cytochrome b is not needed for DCCD inhibition of ubiquinol:cytochrome c oxidoreductase in Rhodobacter sphaeroides chromatophores
    • Shinkarev, V. P., Ugulava, N. B., Takahashi, E., Crofts, A. R., and Wraight, C. A. (2000) Aspartate-187 of cytochrome b is not needed for DCCD inhibition of ubiquinol:cytochrome c oxidoreductase in Rhodobacter sphaeroides chromatophores Biochemistry 39, 14232-14237
    • (2000) Biochemistry , vol.39 , pp. 14232-14237
    • Shinkarev, V.P.1    Ugulava, N.B.2    Takahashi, E.3    Crofts, A.R.4    Wraight, C.A.5
  • 16
    • 0036254366 scopus 로고    scopus 로고
    • 1 complex: Predicted conformational changes and inhibition of proton translocation
    • DOI 10.1023/A:1015132323939
    • 1 complex: Predicted conformational changes and inhibition of proton translocation J. Bioenerg. Biomembr. 34, 81-88 (Pubitemid 34477970)
    • (2002) Journal of Bioenergetics and Biomembranes , vol.34 , Issue.2 , pp. 81-88
    • Wang, Y.1    Beattie, D.S.2
  • 18
    • 0032499644 scopus 로고    scopus 로고
    • A new metal-binding site in photosynthetic bacterial reaction centers that modulates Q(A) to Q(B) electron transfer
    • DOI 10.1021/bi980395n
    • B electron transfer Biochemistry 37, 8278-8281 (Pubitemid 28275446)
    • (1998) Biochemistry , vol.37 , Issue.23 , pp. 8278-8281
    • Utschig, L.M.1    Ohigashi, Y.2    Thurnauer, M.C.3    Tiede, D.M.4
  • 22
    • 34249668338 scopus 로고    scopus 로고
    • Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase
    • DOI 10.1021/bi700173w
    • Qin, L., Mills, D. A., Hiser, C., Murphree, A., Garavito, R. M., Ferguson-Miller, S., and Hosler, J. (2007) Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase Biochemistry 46, 6239-6248 (Pubitemid 46842867)
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6239-6248
    • Qin, L.1    Mills, D.A.2    Hiser, C.3    Murphree, A.4    Michael Garavito, R.5    Ferguson-Miller, S.6    Hosler, J.7
  • 23
    • 0037177829 scopus 로고    scopus 로고
    • Membrane potential-controlled inhibition of cytochrome c oxidase by zinc
    • DOI 10.1074/jbc.M111922200
    • Mills, D. A., Schmidt, B., Hiser, C., Westley, E., and Ferguson-Miller, S. (2002) Membrane potential-controlled inhibition of cytochrome c oxidase by zinc J. Biol. Chem. 277, 14894-14901 (Pubitemid 34952563)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14894-14901
    • Mills, D.A.1    Schmidt, B.2    Hiser, C.3    Westley, E.4    Ferguson-Miller, S.5
  • 29
    • 46649119960 scopus 로고    scopus 로고
    • y fusion complexes reveal the distance constraints for functional electron transfer between photosynthesis components
    • y fusion complexes reveal the distance constraints for functional electron transfer between photosynthesis components J. Biol. Chem. 283, 13973-13982
    • (2008) J. Biol. Chem. , vol.283 , pp. 13973-13982
    • Lee, D.W.1    Ozturk, Y.2    Osyczka, A.3    Cooley, J.W.4    Daldal, F.5
  • 30
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicinchoninic acid Anal. Biochem. 150, 76-85 (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0021758697 scopus 로고
    • Electron and proton transfers through quinones and cytochrome bc complexes
    • Rich, P. R. (1984) Electron and proton transfers through quinones and cytochrome bc complexes Biochim. Biophys. Acta 768, 53-79
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 53-79
    • Rich, P.R.1
  • 33
    • 0025115245 scopus 로고
    • Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c
    • Moss, D., Nabedryk, E., Breton, J., and Mantele, W. (1990) Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c Eur. J. Biochem. 187, 565-572 (Pubitemid 20074919)
    • (1990) European Journal of Biochemistry , vol.187 , Issue.3 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mantele, W.4
  • 34
    • 33745713081 scopus 로고    scopus 로고
    • Study on the redox state dependent γ(CH) vibrational modes of the c-type heme
    • DOI 10.1002/bip.20443
    • Dorr, S., Wolpert, M., and Hellwig, P. (2006) Study on the redox state dependent δ(CH) vibrational modes of the c -type heme Biopolymers 82, 349-352 (Pubitemid 44000902)
    • (2006) Biopolymers , vol.82 , Issue.4 , pp. 349-352
    • Dorr, S.1    Wolpert, M.2    Hellwig, P.3
  • 36
    • 33746628483 scopus 로고    scopus 로고
    • Probing the role of E272 in quinol oxidation of mitochondrial complex III
    • DOI 10.1021/bi060280g
    • Wenz, T., Hellwig, P., MacMillan, F., Meunier, B., and Hunte, C. (2006) Probing the role of E272 in quinol oxidation of mitochondrial complex III Biochemistry 45, 9042-9052 (Pubitemid 44156366)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9042-9052
    • Wenz, T.1    Hellwig, P.2    MacMillan, F.3    Meunier, B.4    Hunte, C.5
  • 39
    • 0028808109 scopus 로고
    • 1 complex by blocking a protonatable group
    • 1 complex by blocking a protonatable group J. Biol. Chem. 270, 25001-25006
    • (1995) J. Biol. Chem. , vol.270 , pp. 25001-25006
    • Link, T.A.1    Von Jagow, G.2
  • 42
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy
    • DOI 10.1021/bi9725576
    • Hellwig, P., Behr, J., Ostermeier, C., Richter, O. M., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H., and Mantele, W. (1998) Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy Biochemistry 37, 7390-7399 (Pubitemid 28235222)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2    Ostermeier, C.3    Richter, O.-M.H.4    Pfitzner, U.5    Odenwald, A.6    Ludwig, B.7    Michel, H.8    Mantele, W.9
  • 43
    • 0142126718 scopus 로고    scopus 로고
    • 1 Complex from Paracoccus denitrificans: Evidence for Protonation Reactions Coupled to Quinone Binding
    • DOI 10.1021/bi035103j
    • 1 complex from Paracoccus denitrificans: Evidence for protonation reactions coupled to quinone binding Biochemistry 42, 12391-12399 (Pubitemid 37296515)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12391-12399
    • Ritter, M.1    Anderka, O.2    Ludwig, B.3    Mantele, W.4    Hellwig, P.5
  • 44
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • DOI 10.1111/j.1745-7270.2007.00320.x
    • Kong, J. and Yu, S. (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures Acta Biochim. Biophys. Sin. 39, 549-559 (Pubitemid 47293710)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.8 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 46
    • 33745713079 scopus 로고    scopus 로고
    • Electrochemically induced FTIR difference spectroscopy in the mid- to far infrared (200 μm) domain: A new setup for the analysis of metal-ligand interactions in redox proteins
    • DOI 10.1002/bip.20469
    • Berthomieu, C., Marboutin, L., Dupeyrat, F., and Bouyer, P. (2006) Electrochemically induced FTIR difference spectroscopy in the mid- to far infrared (200 μm) domain: A new setup for the analysis of metal-ligand interactions in redox proteins Biopolymers 82, 363-367 (Pubitemid 44000905)
    • (2006) Biopolymers , vol.82 , Issue.4 , pp. 363-367
    • Berthomieu, C.1    Marboutin, L.2    Dupeyrat, F.3    Bouyer, P.4
  • 47
    • 0001617001 scopus 로고    scopus 로고
    • Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: Infrared and Raman markers of the protonation state of a histidine side chain
    • Hasegawa, K., Ono, T., and Noguchi, T. (2000) Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: Infrared and Raman markers of the protonation state of a histidine side chain J. Phys. Chem. B 104, 4253-4265
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4253-4265
    • Hasegawa, K.1    Ono, T.2    Noguchi, T.3
  • 50
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • DOI 10.1074/jbc.M108264200
    • Gazaryan, I. G., Krasnikov, B. F., Ashby, G. A., Thorneley, R. N., Kristal, B. S., and Brown, A. M. (2002) Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase J. Biol. Chem. 277, 10064-10072 (Pubitemid 34968116)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.F.4    Kristal, B.S.5    Brown, A.M.6


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