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Volumn 25, Issue 20, 2006, Pages 4963-4970

Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex

Author keywords

Bioenergetics; Membrane proteins; Quinol:fumarate reductase; Transmembrane proton potential; Transmembrane proton transfer

Indexed keywords

FUMARATE REDUCTASE; GLUTAMIC ACID; MEMBRANE PROTEIN; QUINOL FUMARATE REDUCTASE; UNCLASSIFIED DRUG;

EID: 33750218146     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601361     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 11744384413 scopus 로고
    • The Grotthuss mechanism
    • Agmon N (1995) The Grotthuss mechanism. Chem Phys Lett 244: 456-462
    • (1995) Chem Phys Lett , vol.244 , pp. 456-462
    • Agmon, N.1
  • 4
    • 85047700415 scopus 로고    scopus 로고
    • Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes
    • Biel S, Simon J, Groß R, Ruiz T, Ruitenberg M, Kröger A (2002) Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes. Eur J Biochem 269: 1974-1983
    • (2002) Eur J Biochem , vol.269 , pp. 1974-1983
    • Biel, S.1    Simon, J.2    Groß, R.3    Ruiz, T.4    Ruitenberg, M.5    Kröger, A.6
  • 5
    • 0036898073 scopus 로고    scopus 로고
    • The gp91(phox) component of NADPH oxidase is not a voltage-gated proton channel
    • DeCoursey TE, Morgan D, Cherny VV (2002) The gp91(phox) component of NADPH oxidase is not a voltage-gated proton channel. J Gen Physiol 120: 773-779
    • (2002) J Gen Physiol , vol.120 , pp. 773-779
    • DeCoursey, T.E.1    Morgan, D.2    Cherny, V.V.3
  • 6
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén K, Gilderson G, delroth P, Brzezinski P (2005) A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437: 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Delroth, P.3    Brzezinski, P.4
  • 8
    • 0033679563 scopus 로고    scopus 로고
    • Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach
    • Ge Z, Feng Y, Dangler CA, Xu S, Taylor NS, Fox JG (2000) Fumarate reductase is essential for Helicobacter pylori colonization of the mouse stomach. Microb Pathog 29: 279-287
    • (2000) Microb Pathog , vol.29 , pp. 279-287
    • Ge, Z.1    Feng, Y.2    Dangler, C.A.3    Xu, S.4    Taylor, N.S.5    Fox, J.G.6
  • 9
    • 0028218045 scopus 로고
    • The direction of the proton exchange associated with the redox reactions of menaquinone during electron transport in Wolinella succinogenes
    • Geisler V, Ullmann R, Kröger A (1994) The direction of the proton exchange associated with the redox reactions of menaquinone during electron transport in Wolinella succinogenes. Biochim Biophys Acta 1184: 219-226
    • (1994) Biochim Biophys Acta , vol.1184 , pp. 219-226
    • Geisler, V.1    Ullmann, R.2    Kröger, A.3
  • 10
    • 10044230751 scopus 로고    scopus 로고
    • Calculated coupling of transmembrane electron and proton transfer in dihemic quinol:fumarate reductase
    • Haas AH, Lancaster CRD (2004) Calculated coupling of transmembrane electron and proton transfer in dihemic quinol:fumarate reductase. Biophys J 87: 4298-4315
    • (2004) Biophys J , vol.87 , pp. 4298-4315
    • Haas, A.H.1    Lancaster, C.R.D.2
  • 11
    • 27144473873 scopus 로고    scopus 로고
    • FTIR difference spectra of Wolinella succinogenes quinol:-fumarate reductase support a key role of Glu C180 within the 'E-pathway hypothesis' of coupled transmembrane electron and proton transfer
    • Haas AH, Sauer US, Gross R, Simon J, Mäntele W, Lancaster CRD (2005) FTIR difference spectra of Wolinella succinogenes quinol:-fumarate reductase support a key role of Glu C180 within the 'E-pathway hypothesis' of coupled transmembrane electron and proton transfer. Biochemistry 44: 13949-13961
    • (2005) Biochemistry , vol.44 , pp. 13949-13961
    • Haas, A.H.1    Sauer, U.S.2    Gross, R.3    Simon, J.4    Mäntele, W.5    Lancaster, C.R.D.6
  • 12
    • 0030600143 scopus 로고    scopus 로고
    • A structural model for the membrane-integral domain of succinate: Quinone oxidoreductases
    • Hägerhäll C, Hederstedt L (1996) A structural model for the membrane-integral domain of succinate: quinone oxidoreductases. FEBS Lett 389: 25-31
    • (1996) FEBS Lett , vol.389 , pp. 25-31
    • Hägerhäll, C.1    Hederstedt, L.2
  • 13
    • 0036899247 scopus 로고    scopus 로고
    • Proton conduction through gp91(phox)
    • Henderson LM, Meech RW (2002) Proton conduction through gp91(phox). J Gen Physiol 120: 759-765
    • (2002) J Gen Physiol , vol.120 , pp. 759-765
    • Henderson, L.M.1    Meech, R.W.2
  • 14
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka M, Törnroth S, Byrne B, 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    Törnroth, S.2    Byrne, B.3    Iwata, S.4
  • 15
    • 0020407884 scopus 로고
    • Tetraphenylborate-sensitive electrode for measuring membrane potential
    • Karlovsky P, Dadak V (1982) Tetraphenylborate-sensitive electrode for measuring membrane potential. Folia Microbiol 27: 460-464
    • (1982) Folia Microbiol , vol.27 , pp. 460-464
    • Karlovsky, P.1    Dadak, V.2
  • 16
    • 0018183608 scopus 로고
    • Fumarate as terminal acceptor of phosphorylative electron transport
    • Kröger A (1978) Fumarate as terminal acceptor of phosphorylative electron transport. Biochim Biophys Acta 505: 129-145
    • (1978) Biochim Biophys Acta , vol.505 , pp. 129-145
    • Kröger, A.1
  • 17
    • 0037122939 scopus 로고    scopus 로고
    • Fumarate respiration of Wolinella succinogenes: Enzymology, energetics and coupling mechanism
    • Kröger A, Biel S, Simon J, Groß R, Unden G, Lancaster CRD (2002) Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism. Biochim Biophys Acta 1553: 23-38
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 23-38
    • Kröger, A.1    Biel, S.2    Simon, J.3    Groß, R.4    Unden, G.5    Lancaster, C.R.D.6
  • 18
    • 0037064218 scopus 로고    scopus 로고
    • Wolinella succinogenes quinol:fumarate reductase-2.2 Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer
    • Lancaster CRD (2002) Wolinella succinogenes quinol:fumarate reductase-2.2 Å resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer. Biochim Biophys Acta 1565: 215-231
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 215-231
    • Lancaster, C.R.D.1
  • 19
    • 0038392249 scopus 로고    scopus 로고
    • The role of electrostatics in proton-conducting membrane protein complexes
    • Lancaster CRD (2003) The role of electrostatics in proton-conducting membrane protein complexes. FEBS Lett 545: 52-60
    • (2003) FEBS Lett , vol.545 , pp. 52-60
    • Lancaster, C.R.D.1
  • 20
    • 10044274955 scopus 로고    scopus 로고
    • Structure and function of succinate:quinone oxidoreductases and the role of quinol:fumarate reductases in fumarate respiration
    • Zannoni D (ed). The Netherlands, Dordrecht: Kluwer Scientific
    • Lancaster CRD (2004) Structure and function of succinate:quinone oxidoreductases and the role of quinol:fumarate reductases in fumarate respiration. In Respiration in Archaea and Bacteria. Volume 1: Diversity of Prokaryotic Electron Transport Carriers, Zannoni D (ed). The Netherlands, Dordrecht: Kluwer Scientific pp 57-85
    • (2004) Respiration in Archaea and Bacteria. Volume 1: Diversity of Prokaryotic Electron Transport Carriers , pp. 57-85
    • Lancaster, C.R.D.1
  • 21
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
    • Lancaster CRD, Kröger A, Auer M, Michel H (1999) Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution. Nature 402: 377-385
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.D.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 22
    • 0034700104 scopus 로고    scopus 로고
    • Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes
    • Lancaster CRD, Groß R, Haas A, Ritter M, Mäntele W, Simon J, Kröger A (2000) Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes. Proc Natl Acad Sci USA 97: 13051-13056
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13051-13056
    • Lancaster, C.R.D.1    Groß, R.2    Haas, A.3    Ritter, M.4    Mäntele, W.5    Simon, J.6    Kröger, A.7
  • 23
    • 0034831591 scopus 로고    scopus 로고
    • A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction
    • Lancaster CRD, Groß R, Simon J (2001) A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Eur J Biochem 268: 1820-1827
    • (2001) Eur J Biochem , vol.268 , pp. 1820-1827
    • Lancaster, C.R.D.1    Groß, R.2    Simon, J.3
  • 25
    • 0034713845 scopus 로고    scopus 로고
    • The distal heme center in Bacillus subtilis succinate:menaquinone reductase is crucial for electron transfer to menaquinone
    • Matsson M, Tolstoy D, Aasa R, Hederstedt L (2000) The distal heme center in Bacillus subtilis succinate:menaquinone reductase is crucial for electron transfer to menaquinone. Biochemistry 39: 8617-8624
    • (2000) Biochemistry , vol.39 , pp. 8617-8624
    • Matsson, M.1    Tolstoy, D.2    Aasa, R.3    Hederstedt, L.4
  • 26
    • 1842845132 scopus 로고    scopus 로고
    • NOX family NADPH oxidases: Do they have built-in proton channels?
    • Maturana A, Krause KH, Demaurex N (2002) NOX family NADPH oxidases: do they have built-in proton channels? J Gen Physiol 120: 781-786
    • (2002) J Gen Physiol , vol.120 , pp. 781-786
    • Maturana, A.1    Krause, K.H.2    Demaurex, N.3
  • 28
    • 33645568742 scopus 로고    scopus 로고
    • Heterologous production in Wolinella succinogenes and characterisation of the quinol:fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni
    • Mileni M, MacMillan F, Tziatzios C, Zwicker K, Haas AH, Mäntele W, Simon J, Lancaster CRD (2006) Heterologous production in Wolinella succinogenes and characterisation of the quinol:fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni. Biochem J 395: 191-201
    • (2006) Biochem J , vol.395 , pp. 191-201
    • Mileni, M.1    MacMillan, F.2    Tziatzios, C.3    Zwicker, K.4    Haas, A.H.5    Mäntele, W.6    Simon, J.7    Lancaster, C.R.D.8
  • 29
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62: 327-367
    • (1976) J Theor Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 30
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • Mitchell P (1979) Keilin's respiratory chain concept and its chemiosmotic consequences. Science 206: 1148-1159
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 31
    • 23244438766 scopus 로고    scopus 로고
    • Ubiquinol oxidation in the cytochrome bc complex: Reaction mechanism and prevention of short-circuiting
    • Mulkidjanian AY (2005) Ubiquinol oxidation in the cytochrome bc complex: reaction mechanism and prevention of short-circuiting. Biochim Biophys Acta 1709: 5-34
    • (2005) Biochim Biophys Acta , vol.1709 , pp. 5-34
    • Mulkidjanian, A.Y.1
  • 32
    • 33749128697 scopus 로고    scopus 로고
    • Protons at interfaces: Implications for biological energy conversion
    • in press, accessible online as DOI: 10.1016/j.bbabio.2006.02.015
    • Mulkidjanian AY, Heberle J, Cherepanov DA (2006) Protons at interfaces: implications for biological energy conversion, Biochim. Biophys. Acta, in press, accessible online as DOI: 10.1016/j.bbabio.2006.02.015
    • (2006) Biochim. Biophys. Acta
    • Mulkidjanian, A.Y.1    Heberle, J.2    Cherepanov, D.A.3
  • 33
    • 0025854251 scopus 로고
    • 1-complex of Rhodobacter sphaeroides: The electron transfer between cytochrome b hemes can be non-electrogenic
    • 1-complex of Rhodobacter sphaeroides: the electron transfer between cytochrome b hemes can be non-electrogenic. FEBS Lett 284: 227-231
    • (1991) FEBS Lett , vol.284 , pp. 227-231
    • Mulkidjanian, A.Y.1    Mamedov, M.D.2    Drachev, L.A.3
  • 34
    • 0034651685 scopus 로고    scopus 로고
    • Simple redox-linked proton-transfer design: New insights from structures of quinol-fumarate reductase
    • Ohnishi T, Moser CC, Page CC, Dutton PL, Yano T (2000) Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase. Structure 8: R23-R32
    • (2000) Structure , vol.8
    • Ohnishi, T.1    Moser, C.C.2    Page, C.C.3    Dutton, P.L.4    Yano, T.5
  • 35
    • 0037040603 scopus 로고    scopus 로고
    • Structural biology. PMF through the redox loop
    • Richardson D, Sawers G (2002) Structural biology. PMF through the redox loop. Science 295: 1842-1843
    • (2002) Science , vol.295 , pp. 1842-1843
    • Richardson, D.1    Sawers, G.2
  • 36
    • 0032189445 scopus 로고    scopus 로고
    • Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential
    • Schirawski J, Unden G (1998) Menaquinone-dependent succinate dehydrogenase of bacteria catalyzes reversed electron transport driven by the proton potential. Eur J Biochem 257: 210-215
    • (1998) Eur J Biochem , vol.257 , pp. 210-215
    • Schirawski, J.1    Unden, G.2
  • 37
    • 0034819978 scopus 로고    scopus 로고
    • Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase
    • Schnorpfeil M, Janausch IG, Biel S, Kröger A, Unden G (2001) Generation of a proton potential by succinate dehydrogenase of Bacillus subtilis functioning as a fumarate reductase. Eur J Biochem 268: 3069-3074
    • (2001) Eur J Biochem , vol.268 , pp. 3069-3074
    • Schnorpfeil, M.1    Janausch, I.G.2    Biel, S.3    Kröger, A.4    Unden, G.5
  • 38
    • 0002036605 scopus 로고
    • Mémoire sur la decomposition de l'eau et des corps qu'elle tient en dissolution à l'aide de l'electricité galvanique
    • von Grotthuss CJT (1806) Mémoire sur la decomposition de l'eau et des corps qu'elle tient en dissolution à l'aide de l'electricité galvanique. Ann Chim Phys (Paris) 58: 54-74
    • (1806) Ann Chim Phys (Paris) , vol.58 , pp. 54-74
    • Von Grotthuss, C.J.T.1
  • 39
    • 0019783090 scopus 로고
    • Measurement of membrane potential in Bacillus subtilis: A comparison of lipophilic cations, rubidium ion, and cyanine dye as probes
    • Zaritsky A, Kihara M, Macnab RM (1981) Measurement of membrane potential in Bacillus subtilis: a comparison of lipophilic cations, rubidium ion, and cyanine dye as probes. J Membr Biol 63: 215-231
    • (1981) J Membr Biol , vol.63 , pp. 215-231
    • Zaritsky, A.1    Kihara, M.2    Macnab, R.M.3


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