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Volumn 1837, Issue 6, 2014, Pages 750-760

Evidence for interaction between the triheme cytochrome PpcA from Geobacter sulfurreducens and anthrahydroquinone-2,6-disulfonate, an analog of the redox active components of humic substances

Author keywords

AQDS; Electron transfer; Geobacter; Humics; Multiheme cytochromes; NMR

Indexed keywords

ANTHRAHYDROQUINONE 2,6 DISULFONATE; CYTOCHROME; CYTOCHROME PPCA; HEME; HYDROQUINONE DERIVATIVE; NITROGEN 15; UNCLASSIFIED DRUG; ANTHRAHYDROQUINONE-2,6-DISULFONATE; ANTHRAQUINONE DERIVATIVE; ANTHRAQUINONE-2,6-DISULFONATE; HUMIC SUBSTANCE;

EID: 84896689258     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.02.004     Document Type: Article
Times cited : (24)

References (54)
  • 1
    • 78650298909 scopus 로고    scopus 로고
    • In situ to in silico and back: Elucidating the physiology and ecology of Geobacter spp using genome-scale modelling
    • R. Mahadevan, B.O. Palsson, and D.R. Lovley In situ to in silico and back: elucidating the physiology and ecology of Geobacter spp. using genome-scale modelling Nat. Rev. Microbiol. 9 2011 39 50
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 39-50
    • Mahadevan, R.1    Palsson, B.O.2    Lovley, D.R.3
  • 2
    • 0037337606 scopus 로고    scopus 로고
    • Electricity production by Geobacter sulfurreducens attached to electrodes
    • DOI 10.1128/AEM.69.3.1548-1555.2003
    • D.R. Bond, and D.R. Lovley Electricity production by Geobacter sulfurreducens attached to electrodes Appl. Environ. Microbiol. 69 2003 1548 1555 (Pubitemid 36314294)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.3 , pp. 1548-1555
    • Bond, D.R.1    Lovley, D.R.2
  • 3
    • 7044222207 scopus 로고    scopus 로고
    • Dissimilatory Fe(III) and Mn(IV) reduction
    • DOI 10.1016/S0065-2911(04)49005-5, PII S0065291104490055
    • D.R. Lovley, D.E. Holmes, and K.P. Nevin Dissimilatory Fe(III) and Mn(IV) reduction Adv. Microb. Physiol. 49 2004 219 286 (Pubitemid 39424008)
    • (2004) Advances in Microbial Physiology , vol.49 , pp. 219-286
    • Lovley, D.R.1    Holmes, D.E.2    Nevin, K.P.3
  • 4
    • 44349126251 scopus 로고    scopus 로고
    • Extracellular electron transfer: Wires, capacitors, iron lungs, and more
    • DOI 10.1111/j.1472-4669.2008.00148.x
    • D.R. Lovley Extracellular electron transfer: wires, capacitors, iron lungs, and more Geobiology 6 2008 225 231 (Pubitemid 351733124)
    • (2008) Geobiology , vol.6 , Issue.3 , pp. 225-231
    • Lovley, D.R.1
  • 6
    • 27744521813 scopus 로고    scopus 로고
    • Remediation and recovery of uranium from contaminated subsurface environments with electrodes
    • DOI 10.1021/es050457e
    • K.B. Gregory, and D.R. Lovley Remediation and recovery of uranium from contaminated subsurface environments with electrodes Environ. Sci. Technol. 39 2005 8943 8947 (Pubitemid 41636169)
    • (2005) Environmental Science and Technology , vol.39 , Issue.22 , pp. 8943-8947
    • Gregory, K.B.1    Lovley, D.R.2
  • 7
    • 0035369144 scopus 로고    scopus 로고
    • Microbial detoxification of metals and radionuclides
    • DOI 10.1016/S0958-1669(00)00207-X
    • J.R. Lloyd, and D.R. Lovley Microbial detoxification of metals and radionuclides Curr. Opin. Biotechnol. 12 2001 248 253 (Pubitemid 32524336)
    • (2001) Current Opinion in Biotechnology , vol.12 , Issue.3 , pp. 248-253
    • Lloyd, J.R.1    Lovley, D.R.2
  • 8
    • 33748853295 scopus 로고    scopus 로고
    • Microorganisms pumping iron: Anaerobic microbial iron oxidation and reduction
    • DOI 10.1038/nrmicro1490, PII NRMICRO1490
    • K.A. Weber, L.A. Achenbach, and J.D. Coates Microorganisms pumping iron: anaerobic microbial iron oxidation and reduction Nat. Rev. Microbiol. 4 2006 752 764 (Pubitemid 44420126)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.10 , pp. 752-764
    • Weber, K.A.1    Achenbach, L.A.2    Coates, J.D.3
  • 9
    • 0036742036 scopus 로고    scopus 로고
    • Multiple influences of nitrate on uranium solubility during bioremediation of uranium-contaminated subsurface sediments
    • K.T. Finneran, M.E. Housewright, and D.R. Lovley Multiple influences of nitrate on uranium solubility during bioremediation of uranium-contaminated subsurface sediments Environ. Microbiol. 4 2002 510 516
    • (2002) Environ. Microbiol. , vol.4 , pp. 510-516
    • Finneran, K.T.1    Housewright, M.E.2    Lovley, D.R.3
  • 10
    • 0029790133 scopus 로고    scopus 로고
    • Humic substances as electron acceptors for microbial respiration
    • D.R. Lovley, J.D. Coates, and E.L. Blunt-Harris et al. Humic substances as electron acceptors for microbial respiration Nat. (Lett.) 382 1996 445 447
    • (1996) Nat. (Lett.) , vol.382 , pp. 445-447
    • Lovley, D.R.1    Coates, J.D.2    Blunt-Harris, E.L.3
  • 11
    • 0034934202 scopus 로고    scopus 로고
    • Redox properties of standard humic acids
    • DOI 10.1016/S0016-7061(01)00040-4, PII S0016706101000404
    • Z. Struyk, and G. Sposito Redox properties of standard humic acids Geoderma 102 2001 329 346 (Pubitemid 32646423)
    • (2001) Geoderma , vol.102 , Issue.3-4 , pp. 329-346
    • Struyk, Z.1    Sposito, G.2
  • 13
    • 78650170320 scopus 로고    scopus 로고
    • Gene expression and deletion analysis of mechanisms for electron transfer from electrodes to Geobacter sulfurreducens
    • S.M. Strycharz, R.H. Glaven, and M.V. Coppi et al. Gene expression and deletion analysis of mechanisms for electron transfer from electrodes to Geobacter sulfurreducens Bioelectrochemistry 80 2011 142 150
    • (2011) Bioelectrochemistry , vol.80 , pp. 142-150
    • Strycharz, S.M.1    Glaven, R.H.2    Coppi, M.V.3
  • 15
    • 77950283289 scopus 로고    scopus 로고
    • Role of Geobacter sulfurreducens outer surface c-type cytochromes in reduction of soil humic acid and anthraquinone-2,6-disulfonate
    • J.W. Voordeckers, B.C. Kim, and M. Izallalen et al. Role of Geobacter sulfurreducens outer surface c-type cytochromes in reduction of soil humic acid and anthraquinone-2,6-disulfonate Appl. Environ. Microbiol. 76 2010 2371 2375
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2371-2375
    • Voordeckers, J.W.1    Kim, B.C.2    Izallalen, M.3
  • 17
    • 77956173875 scopus 로고    scopus 로고
    • The humic acid analogue antraquinone-2,6-disulfonate (AQDS) serves as an electron shuttle in the electricity-driven microbial dechlorination of trichloroethene to cis-dichloroethene
    • F. Aulenta, V.D. Maio, and T. Ferri et al. The humic acid analogue antraquinone-2,6-disulfonate (AQDS) serves as an electron shuttle in the electricity-driven microbial dechlorination of trichloroethene to cis-dichloroethene Bioresour. Technol. 101 2010 9728 9733
    • (2010) Bioresour. Technol. , vol.101 , pp. 9728-9733
    • Aulenta, F.1    Maio, V.D.2    Ferri, T.3
  • 18
    • 0036250038 scopus 로고    scopus 로고
    • Diversity and ubiquity of bacteria capable of utilizing humic substances as electron donors for anaerobic respiration
    • DOI 10.1128/AEM.68.5.2445-2452.2002
    • J.D. Coates, K.A. Cole, and R. Chakraborty et al. Diversity and ubiquity of bacteria capable of utilizing humic substances as electron donors for anaerobic respiration Appl. Environ. Microbiol. 68 2002 2445 2452 (Pubitemid 34477843)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.5 , pp. 2445-2452
    • Coates, J.D.1    Cole, K.A.2    Chakraborty, R.3    O'Connor, S.M.4    Achenbach, L.A.5
  • 21
    • 49349107641 scopus 로고    scopus 로고
    • Structural insights into the modulation of the redox properties of two Geobacter sulfurreducens homologous triheme cytochromes
    • L. Morgado, M. Bruix, and V. Orshonsky et al. Structural insights into the modulation of the redox properties of two Geobacter sulfurreducens homologous triheme cytochromes Biochim. Biophys. Acta 1777 2008 1157 1165
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1157-1165
    • Morgado, L.1    Bruix, M.2    Orshonsky, V.3
  • 22
    • 82355175841 scopus 로고    scopus 로고
    • Revealing the structural origin of the redox-Bohr effect: The first solution structure of a cytochrome from Geobacter sulfurreducens
    • L. Morgado, V.B. Paixão, and M. Schiffer et al. Revealing the structural origin of the redox-Bohr effect: the first solution structure of a cytochrome from Geobacter sulfurreducens Biochem. J. 441 2012 179 187
    • (2012) Biochem. J. , vol.441 , pp. 179-187
    • Morgado, L.1    Paixão, V.B.2    Schiffer, M.3
  • 26
    • 77954380092 scopus 로고    scopus 로고
    • Thermodynamic characterization of a triheme cytochrome family from Geobacter sulfurreducens reveals mechanistic and functional diversity
    • L. Morgado, M. Bruix, and M. Pessanha et al. Thermodynamic characterization of a triheme cytochrome family from Geobacter sulfurreducens reveals mechanistic and functional diversity Biophys. J. 99 2010 293 301
    • (2010) Biophys. J. , vol.99 , pp. 293-301
    • Morgado, L.1    Bruix, M.2    Pessanha, M.3
  • 28
    • 84864936443 scopus 로고    scopus 로고
    • Fine tuning of redox networks on multiheme cytochromes from Geobacter sulfurreducens drives physiological electron/proton energy transduction
    • L. Morgado, J.M. Dantas, and M. Bruix et al. Fine tuning of redox networks on multiheme cytochromes from Geobacter sulfurreducens drives physiological electron/proton energy transduction Bioinorg. Chem. Appl. 2012 2012 1-9
    • (2012) Bioinorg. Chem. Appl. , vol.2012 , pp. 1-9
    • Morgado, L.1    Dantas, J.M.2    Bruix, M.3
  • 29
    • 0036186071 scopus 로고    scopus 로고
    • Protective role of tolC in efflux of the electron shuttle anthraquinone-2,6-disulfonate
    • DOI 10.1128/JB.184.6.1806-1810.2002
    • J.B. Shyu, D.P. Lies, and D.K. Newman Protective role of tolC in efflux of the electron shuttle anthraquinone-2,6-disulfonate J. Bacteriol. 184 2002 1806 1810 (Pubitemid 34188237)
    • (2002) Journal of Bacteriology , vol.184 , Issue.6 , pp. 1806-1810
    • Shyu, J.B.H.1    Lies, D.P.2    Newman, D.K.3
  • 30
    • 40849087788 scopus 로고    scopus 로고
    • Isotopic labeling of c-type multiheme cytochromes overexpressed in E. Coli
    • A.P. Fernandes, I. Couto, and L. Morgado et al. Isotopic labeling of c-type multiheme cytochromes overexpressed in E. coli Protein Expr. Purif. 59 2008 182 188
    • (2008) Protein Expr. Purif. , vol.59 , pp. 182-188
    • Fernandes, A.P.1    Couto, I.2    Morgado, L.3
  • 33
    • 0032448328 scopus 로고    scopus 로고
    • A periplasmic and extracellular c-type cytochrome of Geobacter sulfurreducens acts as a ferric iron reductase and as an electron carrier to other acceptors or to partner bacteria
    • S. Seeliger, R. Cord-Ruwisch, and B. Schink A periplasmic and extracellular c-type \cytochrome of Geobacter sulfurreducens acts as a ferric iron reductase and as an electron carrier to other acceptors or to partner bacteria J. Bacteriol. 180 1998 3686 3691 (Pubitemid 29115101)
    • (1998) Journal of Bacteriology , vol.180 , Issue.14 , pp. 3686-3691
    • Seeliger, S.1    Cord-Ruwisch, R.2    Schink, B.3
  • 34
    • 0015207696 scopus 로고
    • The acceptor specificity of flavins and flavoproteins. I. Techniques for anaerobic spectrophotometry
    • M. Dixon The acceptor specificity of flavins and flavoproteins. I. Techniques for anaerobic spectrophotometry Biochim. Biophys. Acta Bioenerg. 226 1971 241 258
    • (1971) Biochim. Biophys. Acta Bioenerg. , vol.226 , pp. 241-258
    • Dixon, M.1
  • 35
    • 0029181728 scopus 로고
    • 1H, 13C and 15 N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • D.S. Wishart, C.G. Bigam, and A. Holm et al. 1H, 13C and 15 N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects J. Biomol. NMR 5 1995 67 81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3
  • 36
    • 77949262353 scopus 로고    scopus 로고
    • One simple step in the identification of the cofactors signals, one giant leap for the solution structure determination of multiheme proteins
    • L. Morgado, A.P. Fernandes, and Y.Y. Londer et al. One simple step in the identification of the cofactors signals, one giant leap for the solution structure determination of multiheme proteins Biochem. Biophys. Res. Commun. 393 2010 466 470
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 466-470
    • Morgado, L.1    Fernandes, A.P.2    Londer, Y.Y.3
  • 37
    • 35848958773 scopus 로고    scopus 로고
    • Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions
    • DOI 10.1007/s10858-007-9197-z
    • F.H. Schumann, H. Riepl, and T. Maurer et al. Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions J. Biomol. NMR 39 2007 275 289 (Pubitemid 350055750)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.4 , pp. 275-289
    • Schumann, F.H.1    Riepl, H.2    Maurer, T.3    Gronwald, W.4    Neidig, K.-P.5    Kalbitzer, H.R.6
  • 38
    • 66449110287 scopus 로고    scopus 로고
    • DOCK 6: Combining techniques to model RNA-small molecule complexes
    • P.T. Lang, S.R. Brozell, and S. Mukherjee et al. DOCK 6: combining techniques to model RNA-small molecule complexes RNA 15 2009 1219 1230
    • (2009) RNA , vol.15 , pp. 1219-1230
    • Lang, P.T.1    Brozell, S.R.2    Mukherjee, S.3
  • 39
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • E.F. Pettersen, T.D. Goddard, and C.C. Huang et al. UCSF Chimera - a visualization system for exploratory research and analysis J. Comput. Chem. 25 2004 1605 1612
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3
  • 40
    • 8444232122 scopus 로고    scopus 로고
    • Transient complexes of redox proteins: Structural and dynamic details from NMR studies
    • DOI 10.1002/jmr.686
    • M. Prudêncio, and M. Ubbink Transient complexes of redox proteins: structural and dynamic details from NMR studies J. Mol. Recognit. 17 2004 524 539 (Pubitemid 39484220)
    • (2004) Journal of Molecular Recognition , vol.17 , Issue.6 , pp. 524-539
    • Prudencio, M.1    Ubbink, M.2
  • 41
    • 80054977388 scopus 로고    scopus 로고
    • Efficient electron transfer in a protein network lacking specific interactions
    • F. Meschi, F. Wiertz, and L. Klauss et al. Efficient electron transfer in a protein network lacking specific interactions J. Am. Chem. Soc. 133 2011 16861 16867
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16861-16867
    • Meschi, F.1    Wiertz, F.2    Klauss, L.3
  • 42
    • 79961078111 scopus 로고    scopus 로고
    • NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase
    • K. Sakamoto, M. Kamiya, and M. Imai et al. NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase Proc. Natl. Acad. Sci. U. S. A. 108 2011 12271 12276
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12271-12276
    • Sakamoto, K.1    Kamiya, M.2    Imai, M.3
  • 43
    • 32344431599 scopus 로고    scopus 로고
    • 3 with [NiFe] hydrogenase from desulfovibrio vulgaris Miyazaki F
    • DOI 10.1021/bi0514360
    • N. Yahata, T. Saitoh, and Y. Takayama et al. Redox interaction of cytochrome c(3) with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F Biochemistry 45 2006 1653 1662 (Pubitemid 43222109)
    • (2006) Biochemistry , vol.45 , Issue.6 , pp. 1653-1662
    • Yahata, N.1    Saitoh, T.2    Takayama, Y.3    Ozawa, K.4    Ogata, H.5    Higuchi, Y.6    Akutsu, H.7
  • 44
    • 54549114308 scopus 로고    scopus 로고
    • Proteome of Geobacter sulfurreducens grown with Fe(III) oxide or Fe(III) citrate as the electron acceptor
    • Y.H. Ding, K.K. Hixson, and M.A. Aklujkar et al. Proteome of Geobacter sulfurreducens grown with Fe(III) oxide or Fe(III) citrate as the electron acceptor Biochim. Biophys. Acta 1784 2008 1935 1941
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1935-1941
    • Ding, Y.H.1    Hixson, K.K.2    Aklujkar, M.A.3
  • 46
    • 0028812049 scopus 로고
    • Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure
    • D.L. Turner, C.A. Salgueiro, and P. Schenkels et al. Carbon-13 NMR studies of the influence of axial ligand orientation on haem electronic structure Biochim. Biophys. Acta 1246 1995 24 28
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 24-28
    • Turner, D.L.1    Salgueiro, C.A.2    Schenkels, P.3
  • 47
    • 84862893147 scopus 로고    scopus 로고
    • Protein camouflage in cytochrome c-calixarene complexes
    • R.E. McGovern, H. Fernandes, and A.R. Khan et al. Protein camouflage in cytochrome c-calixarene complexes Nat. Chem. 4 2012 527 533
    • (2012) Nat. Chem. , vol.4 , pp. 527-533
    • McGovern, R.E.1    Fernandes, H.2    Khan, A.R.3
  • 48
    • 55949123477 scopus 로고    scopus 로고
    • Stability and structural recovery of the tetramerization domain of p53-R337H mutant induced by a designed templating ligand
    • S. Gordo, V. Martos, and E. Santos et al. Stability and structural recovery of the tetramerization domain of p53-R337H mutant induced by a designed templating ligand Proc. Natl. Acad. Sci. U. S. A. 105 2008 16426 16431
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16426-16431
    • Gordo, S.1    Martos, V.2    Santos, E.3
  • 49
    • 67649757190 scopus 로고    scopus 로고
    • Molecular recognition and self-assembly special feature: Calix[4]arene-based conical-shaped ligands for voltage-dependent potassium channels
    • V. Martos, S.C. Bell, and E. Santos et al. Molecular recognition and self-assembly special feature: calix[4]arene-based conical-shaped ligands for voltage-dependent potassium channels Proc. Natl. Acad. Sci. U. S. A. 106 2009 10482 10486
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10482-10486
    • Martos, V.1    Bell, S.C.2    Santos, E.3
  • 50
    • 4043055221 scopus 로고    scopus 로고
    • Complexes of photosynthetic redox proteins studied by NMR
    • DOI 10.1023/B:PRES.0000036880.67124.e7
    • M. Ubbink Complexes of photosynthetic redox proteins studied by NMR Photosynth. Res. 81 2004 277 287 (Pubitemid 39059690)
    • (2004) Photosynthesis Research , vol.81 , Issue.3 , pp. 277-287
    • Ubbink, M.1
  • 51
    • 79955054283 scopus 로고    scopus 로고
    • Dynamics in electron transfer protein complexes
    • Q. Bashir, S. Scanu, and M. Ubbink Dynamics in electron transfer protein complexes FEBS J. 278 2011 1391 1400
    • (2011) FEBS J. , vol.278 , pp. 1391-1400
    • Bashir, Q.1    Scanu, S.2    Ubbink, M.3
  • 52
    • 79957744584 scopus 로고    scopus 로고
    • Computer review of ChemDraw Ultra 12.0
    • K.R. Cousins Computer review of ChemDraw Ultra 12.0 J. Am. Chem. Soc. 133 2011 8388
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8388
    • Cousins, K.R.1
  • 53
    • 0024289471 scopus 로고
    • Nomenclature of tetrapyrroles. Recommendations 1986 IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN)
    • G.P. Moss Nomenclature of tetrapyrroles. Recommendations 1986 IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN) Eur. J. Biochem. 178 1988 277 328
    • (1988) Eur. J. Biochem. , vol.178 , pp. 277-328
    • Moss, G.P.1


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