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Volumn 1837, Issue 6, 2014, Pages 920-928

Thermodynamic and kinetic characterization of two methyl-accepting chemotaxis heme sensors from Geobacter sulfurreducens reveals the structural origin of their functional difference

Author keywords

c Type heme sensor; Electron transfer kinetics; Geobacter; Redox potential; Signal transduction

Indexed keywords

DITHIONITE; HEME; METHIONINE; BACTERIAL PROTEIN;

EID: 84897122795     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.01.008     Document Type: Article
Times cited : (5)

References (41)
  • 1
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • DOI 10.1016/S0968-0004(01)01852-7, PII S0968000401018527
    • A.H. West, and A.M. Stock Histidine kinases and response regulator proteins in two-component signaling systems Trends Biochem. Sci. 26 2001 369 376 (Pubitemid 32530655)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.6 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 3
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: Bacterial chemotaxis
    • DOI 10.1038/nrm1524
    • G.H. Wadhams, and J.P. Armitage Making sense of it all: bacterial chemotaxis Nat. Rev. Mol. Cell Biol. 5 2004 1024 1037 (Pubitemid 39611538)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.12 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 4
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA
    • S. Aono Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA Acc. Chem. Res. 36 2003 825 831
    • (2003) Acc. Chem. Res. , vol.36 , pp. 825-831
    • Aono, S.1
  • 5
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by heme-containing PAS-domain proteins
    • DOI 10.1152/japplphysiol.00941.2003
    • M.A. Gilles-Gonzalez, and G. Gonzalez Signal transduction by heme-containing PAS-domain proteins J. Appl. Physiol. 96 2004 774 783 (Pubitemid 38140186)
    • (2004) Journal of Applied Physiology , vol.96 , Issue.2 , pp. 774-783
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 6
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • DOI 10.1016/j.jinorgbio.2004.11.006, PII S0162013404003502, Heme-Diatomic Interactions, Part 1
    • M.A. Gilles-Gonzalez, and G. Gonzalez Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses J. Inorg. Biochem. 99 2005 1 22 (Pubitemid 39642968)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 1-22
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 7
    • 10444220187 scopus 로고    scopus 로고
    • CooA, a paradigm for gas sensing regulatory proteins
    • DOI 10.1016/j.jinorgbio.2004.10.032, PII S0162013404003393, Heme-Diatomic Interactions, Part 1
    • G.P. Roberts, R.L. Kerby, H. Youn, and M. Conrad CooA, a paradigm for gas sensing regulatory proteins J. Inorg. Biochem. 99 2005 280 292 (Pubitemid 39642982)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 280-292
    • Roberts, G.P.1    Kerby, R.L.2    Youn, H.3    Conrad, M.4
  • 8
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • DOI 10.1016/j.cbpa.2005.08.015, PII S1367593105001122, Mechanisms / Analytical Techniques
    • E.M. Boon, and M.A. Marletta Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins Curr. Opin. Chem. Biol. 9 2005 441 446 (Pubitemid 41338195)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.5 , pp. 441-446
    • Boon, E.M.1    Marletta, M.A.2
  • 9
    • 33344477903 scopus 로고    scopus 로고
    • Structure-function relationships of EcDOS, a heme-regulated phosphodiesterase from Escherichia coli
    • Y. Sasakura, T. Yoshimura-Suzuki, H. Kurokawa, and T. Shimizu Structure-function relationships of EcDOS, a heme-regulated phosphodiesterase from Escherichia coli Acc. Chem. Res. 39 2006 37 43
    • (2006) Acc. Chem. Res. , vol.39 , pp. 37-43
    • Sasakura, Y.1    Yoshimura-Suzuki, T.2    Kurokawa, H.3    Shimizu, T.4
  • 10
    • 45149083640 scopus 로고    scopus 로고
    • Metal-containing sensor proteins sensing diatomic gas molecules
    • S. Aono Metal-containing sensor proteins sensing diatomic gas molecules Dalton Trans. 2008 3137 3146
    • (2008) Dalton Trans. , pp. 3137-3146
    • Aono, S.1
  • 12
    • 84862760868 scopus 로고    scopus 로고
    • Environmental heme-based sensor proteins: Implications for understanding bacterial pathogenesis
    • A. Farhana, V. Saini, A. Kumar, J.R. Lancaster Jr., and A.J. Steyn Environmental heme-based sensor proteins: implications for understanding bacterial pathogenesis Antioxid. Redox Signal. 17 2012 1232 1245
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1232-1245
    • Farhana, A.1    Saini, V.2    Kumar, A.3    Lancaster, Jr.J.R.4    Steyn, A.J.5
  • 14
    • 33646231481 scopus 로고    scopus 로고
    • Characterization of a c-type heme-containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria
    • Y.Y. Londer, I.S. Dementieva, C.A. D'Ausilio, P.R. Pokkuluri, and M. Schiffer Characterization of a c-type heme-containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria FEMS Microbiol. Lett. 258 2006 173 181
    • (2006) FEMS Microbiol. Lett. , vol.258 , pp. 173-181
    • Londer, Y.Y.1    Dementieva, I.S.2    D'Ausilio, C.A.3    Pokkuluri, P.R.4    Schiffer, M.5
  • 15
    • 0028012225 scopus 로고
    • DcrA, a c-type heme-containing methyl-accepting protein from Desulfovibrio vulgaris hildenborough, senses the oxygen concentration or redox potential of the environment
    • R. Fu, J.D. Wall, and G. Voordouw DcrA, a c-type heme-containing methyl-accepting protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment J. Bacteriol. 176 1994 344 350 (Pubitemid 24034051)
    • (1994) Journal of Bacteriology , vol.176 , Issue.2 , pp. 344-350
    • Fu, R.1    Wall, J.D.2    Voordouw, G.3
  • 16
    • 28044447426 scopus 로고    scopus 로고
    • Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA
    • DOI 10.1021/bi0513352
    • S. Yoshioka, K. Kobayashi, H. Yoshimura, T. Uchida, T. Kitagawa, and S. Aono Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA Biochemistry 44 2005 15406 15413 (Pubitemid 41683135)
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15406-15413
    • Yoshioka, S.1    Kobayashi, K.2    Yoshimura, H.3    Uchida, T.4    Kitagawa, T.5    Aono, S.6
  • 17
    • 40949155089 scopus 로고    scopus 로고
    • Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: Implications for signal transduction
    • P.R. Pokkuluri, M. Pessanha, Y.Y. Londer, S.J. Wood, N.E. Duke, R. Wilton, T. Catarino, C.A. Salgueiro, and M. Schiffer Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: implications for signal transduction J. Mol. Biol. 377 2008 1498 1517
    • (2008) J. Mol. Biol. , vol.377 , pp. 1498-1517
    • Pokkuluri, P.R.1    Pessanha, M.2    Londer, Y.Y.3    Wood, S.J.4    Duke, N.E.5    Wilton, R.6    Catarino, T.7    Salgueiro, C.A.8    Schiffer, M.9
  • 18
    • 84866983174 scopus 로고    scopus 로고
    • Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors
    • M.A. Silva, T.G. Lucas, C.A. Salgueiro, and C.M. Gomes Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors PLoS One 7 2012 e46328
    • (2012) PLoS One , vol.7 , pp. 46328
    • Silva, M.A.1    Lucas, T.G.2    Salgueiro, C.A.3    Gomes, C.M.4
  • 20
    • 18444376154 scopus 로고    scopus 로고
    • Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
    • DOI 10.1111/j.1742-4658.2005.04649.x
    • C.A. Salgueiro, L. Morgado, B. Fonseca, P. Lamosa, T. Catarino, D.L. Turner, and R.O. Louro Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein FEBS J. 272 2005 2251 2260 (Pubitemid 40646795)
    • (2005) FEBS Journal , vol.272 , Issue.9 , pp. 2251-2260
    • Salgueiro, C.A.1    Morgado, L.2    Fonseca, B.3    Lamosa, P.4    Catarino, T.5    Turner, D.L.6    Louro, R.O.7
  • 21
    • 0035814137 scopus 로고    scopus 로고
    • 3: The importance of mechano-chemical coupling for energy transduction
    • R.O. Louro, T. Catarino, J. LeGall, D.L. Turner, and A.V. Xavier Cooperativity between electrons and protons in a monomeric cytochrome c(3): the importance of mechano-chemical coupling for energy transduction ChemBioChem 2 2001 831 837 (Pubitemid 33722675)
    • (2001) ChemBioChem , vol.2 , Issue.11 , pp. 831-837
    • Xavier, A.V.1
  • 22
    • 33751207759 scopus 로고    scopus 로고
    • + energy transduction
    • DOI 10.1021/bi061394v
    • M. Pessanha, L. Morgado, R.O. Louro, Y.Y. Londer, P.R. Pokkuluri, M. Schiffer, and C.A. Salgueiro Thermodynamic characterization of triheme cytochrome PpcA from Geobacter sulfurreducens: evidence for a role played in e(-)/H + energy transduction Biochemistry 45 2006 13910 13917 (Pubitemid 44788759)
    • (2006) Biochemistry , vol.45 , Issue.46 , pp. 13910-13917
    • Pessanha, M.1    Morgado, L.2    Louro, R.O.3    Londer, Y.Y.4    Pokkuluri, P.R.5    Schiffer, M.6    Salgueiro, C.A.7
  • 23
    • 3342967677 scopus 로고    scopus 로고
    • 7 physiological relevance of the conserved residue F15 probed by site-specific mutagenesis
    • DOI 10.1021/bi0492859
    • M. Pessanha, Y.Y. Londer, W.C. Long, J. Erickson, P.R. Pokkuluri, M. Schiffer, and C.A. Salgueiro Redox characterization of Geobacter sulfurreducens cytochrome c(7): physiological relevance of the conserved residue F15 probed by site-specific mutagenesis Biochemistry 43 2004 9909 9917 (Pubitemid 38993840)
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9909-9917
    • Pessanha, M.1    Londer, Y.Y.2    Long, W.C.3    Erickson, J.4    Rokkuluri, P.R.5    Schiffer, M.6    Salgueiroy, C.A.7
  • 24
    • 84875943702 scopus 로고    scopus 로고
    • Relative importance of driving force and electrostatic interactions in the reduction of multihaem cytochromes by small molecules
    • P.O. Quintas, A.P. Cepeda, N. Borges, T. Catarino, and D.L. Turner Relative importance of driving force and electrostatic interactions in the reduction of multihaem cytochromes by small molecules Biochim. Biophys. Acta 1827 2013 745 750
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 745-750
    • Quintas, P.O.1    Cepeda, A.P.2    Borges, N.3    Catarino, T.4    Turner, D.L.5
  • 25
    • 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 226 1971 241 258
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 241-258
    • Dixon, M.1
  • 26
    • 0015910074 scopus 로고
    • The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite
    • D.O. Lambeth, and G. Palmer The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite J. Biol. Chem. 248 1973 6095 6103
    • (1973) J. Biol. Chem. , vol.248 , pp. 6095-6103
    • Lambeth, D.O.1    Palmer, G.2
  • 27
    • 0017004534 scopus 로고
    • Metalloprotein electron transfer reactions: Analysis of reactivity of horse heart cytochrome c with inorganic complexes
    • S. Wherland, and H.B. Gray Metalloprotein electron transfer reactions: analysis of reactivity of horse heart cytochrome c with inorganic complexes Proc. Natl. Acad. Sci. U. S. A. 73 1976 2950 2954
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2950-2954
    • Wherland, S.1    Gray, H.B.2
  • 28
    • 0345338343 scopus 로고
    • Outer-sphere dithionite reductions of metal complexes
    • R.J. Balahura, and M.D. Johnson Outer-sphere dithionite reductions of metal complexes Inorg. Chem. 26 1987 3860 3863
    • (1987) Inorg. Chem. , vol.26 , pp. 3860-3863
    • Balahura, R.J.1    Johnson, M.D.2
  • 30
    • 0027380839 scopus 로고
    • Dissimilatory metal reduction
    • D.R. Lovley Dissimilatory metal reduction Annu. Rev. Microbiol. 47 1993 263 290 (Pubitemid 23302935)
    • (1993) Annual Review of Microbiology , vol.47 , pp. 263-290
    • Lovley, D.R.1
  • 31
    • 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
  • 34
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • P.L. Dutton Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems Methods Enzymol. 54 1978 411 435
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 35
    • 0011741857 scopus 로고
    • - In aqueous solutions. Pulse radiolytic and cyclic voltammetric studies
    • - in aqueous solutions. Pulse radiolytic and cyclic voltammetric studies J. Phys. Chem. 91 1987 1606 1611
    • (1987) J. Phys. Chem. , vol.91 , pp. 1606-1611
    • Neta, P.1    Huie, R.E.2    Harriman, A.3
  • 37
    • 34247868775 scopus 로고    scopus 로고
    • Calculation of redox properties: Understanding short- and long-range effects in rubredoxin
    • DOI 10.1021/jp067387y
    • M. Sulpizi, S. Raugei, J. VandeVondele, P. Carloni, and M. Sprik Calculation of redox properties: understanding short- and long-range effects in rubredoxin J. Phys. Chem. B 111 2007 3969 3976 (Pubitemid 46693358)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.15 , pp. 3969-3976
    • Sulpizi, M.1    Raugei, S.2    VandeVondele, J.3    Carloni, P.4    Sprik, M.5
  • 39
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 40
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55 (29-32) (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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