메뉴 건너뛰기




Volumn 188, Issue 13, 2006, Pages 4705-4714

Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1

Author keywords

[No Author keywords available]

Indexed keywords

4',5' BIS(1,3,2 DITHIOARSOLAN 2 YL)FLUORESCEIN BIS(1,2 ETHANEDITHIOL); CYTOCHROME C; DITHIOL DERIVATIVE; FERRIC ION; IRON; MANGANESE; MTRC PROTEIN; NITRILOTRIACETIC ACID; OMCA PROTEIN; UNCLASSIFIED DRUG;

EID: 33745449038     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01966-05     Document Type: Article
Times cited : (226)

References (41)
  • 1
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams, S. R., R. E. Campbell, L. A. Gross, B. R. Martin, G. K. Walkup, Y. Yao, J. Llopis, and R. Y. Tsien. 2002. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc. 124:6063-6076.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 2
    • 33750622183 scopus 로고
    • Cytochromes: Bacterial
    • Bartsch, R. G. 1971. Cytochromes: bacterial. Methods Enzymol. 34:344-363.
    • (1971) Methods Enzymol. , vol.34 , pp. 344-363
    • Bartsch, R.G.1
  • 3
    • 0031754775 scopus 로고    scopus 로고
    • Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction
    • Beliaev, A. S., and D. A. Saffarini. 1998. Shewanella putrefaciens mtrB encodes an outer membrane protein required for Fe(III) and Mn(IV) reduction. J. Bacteriol. 180:6292-6297.
    • (1998) J. Bacteriol. , vol.180 , pp. 6292-6297
    • Beliaev, A.S.1    Saffarini, D.A.2
  • 4
    • 0035131413 scopus 로고    scopus 로고
    • MtrC, an outer membrane decahaem c cytochrome required for metal reduction in Shewanella putrefaciens MR-1
    • Beliaev, A. S., D. A. Saffarini, J. L. McLaughlin, and D. Hunnicutt. 2001. MtrC, an outer membrane decahaem c cytochrome required for metal reduction in Shewanella putrefaciens MR-1. Mol. Microbiol. 39:722-730.
    • (2001) Mol. Microbiol. , vol.39 , pp. 722-730
    • Beliaev, A.S.1    Saffarini, D.A.2    McLaughlin, J.L.3    Hunnicutt, D.4
  • 5
    • 15444381327 scopus 로고    scopus 로고
    • Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase
    • Chen, B., M. U. Mayer, and T. C. Squier. 2005. Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase. Biochemistry 44:4737-4747.
    • (2005) Biochemistry , vol.44 , pp. 4737-4747
    • Chen, B.1    Mayer, M.U.2    Squier, T.C.3
  • 6
    • 0027174668 scopus 로고
    • A comparison of bathophenanthrolinedisulfonic acid and Ferrozine as chelators of iron(II) in reduction reactions
    • Cowart, R. E., F. L. Singleton, and J. S. Hind. 1993. A comparison of bathophenanthrolinedisulfonic acid and Ferrozine as chelators of iron(II) in reduction reactions. Anal. Biochem. 211:151-155.
    • (1993) Anal. Biochem. , vol.211 , pp. 151-155
    • Cowart, R.E.1    Singleton, F.L.2    Hind, J.S.3
  • 9
    • 0034708830 scopus 로고    scopus 로고
    • Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina NCIMB400
    • Field, S. J., P. S. Dobbin, M. R. Cheesman, N. J. Watmough, A. J. Thomson, and D. J. Richardson. 2000. Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina NCIMB400. J. Biol. Chem. 275:8515-8522.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8515-8522
    • Field, S.J.1    Dobbin, P.S.2    Cheesman, M.R.3    Watmough, N.J.4    Thomson, A.J.5    Richardson, D.J.6
  • 10
    • 0031664567 scopus 로고    scopus 로고
    • Localization and solubilization of the iron(III) reductase of Geobacter sulfurreducens
    • Gaspard, S., F. Vazquez, and C. Holliger. 1998. Localization and solubilization of the iron(III) reductase of Geobacter sulfurreducens. Appl. Environ. Microbiol. 64:3188-3194.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3188-3194
    • Gaspard, S.1    Vazquez, F.2    Holliger, C.3
  • 11
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., S. R. Adams, and R. Y. Tsien. 1998. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281:269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 14
    • 0034610401 scopus 로고    scopus 로고
    • Preferential binding of equine ferricytochrome c to the bacterial photosynthetic reaction center from Rhodobacter sphaeroides
    • Larson, J. W., and C. A. Wraight. 2000. Preferential binding of equine ferricytochrome c to the bacterial photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 39:14822-14830.
    • (2000) Biochemistry , vol.39 , pp. 14822-14830
    • Larson, J.W.1    Wraight, C.A.2
  • 15
    • 0038541683 scopus 로고    scopus 로고
    • Microbial reduction of metals and radionuclides
    • Lloyd, J. R. 2003. Microbial reduction of metals and radionuclides. FEMS Microbiol. Rev. 27:411-425.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 411-425
    • Lloyd, J.R.1
  • 17
    • 33644811688 scopus 로고    scopus 로고
    • One-step, non-denaturing isolation of an RNA polymerase enzyme complex using an improved multi-use affinity probe resin
    • Mayer, M. U., L. Shi, and T. C. Squier. 2005. One-step, non-denaturing isolation of an RNA polymerase enzyme complex using an improved multi-use affinity probe resin. Mol. BioSystems 1:53-56.
    • (2005) Mol. BioSystems , vol.1 , pp. 53-56
    • Mayer, M.U.1    Shi, L.2    Squier, T.C.3
  • 18
    • 1842631445 scopus 로고    scopus 로고
    • Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble, cytochromes
    • Meyer, T. E., A. I. Tsapin, I. Vandenberghe, L. de Smet, D. Frishman, K. H. Nealson, M. A. Cusanovich, and J. J. van Beeumen. 2004. Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble, cytochromes. Omics 8:57-77.
    • (2004) Omics , vol.8 , pp. 57-77
    • Meyer, T.E.1    Tsapin, A.I.2    Vandenberghe, I.3    De Smet, L.4    Frishman, D.5    Nealson, K.H.6    Cusanovich, M.A.7    Van Beeumen, J.J.8
  • 19
    • 0026740398 scopus 로고
    • Localization of cytochromes to the outer membrane of anaerobically grown Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1992. Localization of cytochromes to the outer membrane of anaerobically grown Shewanella putrefaciens MR-1. J. Bacteriol. 174:3429-3438.
    • (1992) J. Bacteriol. , vol.174 , pp. 3429-3438
    • Myers, C.R.1    Myers, J.M.2
  • 20
    • 0030903069 scopus 로고    scopus 로고
    • Outer membrane cytochromes of Shewanella putrefaciens MR-1: Spectral analysis, and purification of the 83-kDa c-type cytochrome
    • Myers, C. R., and J. M. Myers. 1997. Outer membrane cytochromes of Shewanella putrefaciens MR-1: spectral analysis, and purification of the 83-kDa c-type cytochrome. Biochim. Biophys. Acta 1326:307-318.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 307-318
    • Myers, C.R.1    Myers, J.M.2
  • 21
    • 0036271921 scopus 로고    scopus 로고
    • Genetic complementation of an outer membrane cytochrome omcB mutant of Shewanella putrefaciens MR-1 requires omcB plus downstream DNA
    • Myers, J. M., and C. R. Myers. 2002. Genetic complementation of an outer membrane cytochrome omcB mutant of Shewanella putrefaciens MR-1 requires omcB plus downstream DNA. Appl. Environ. Microbiol. 68:2781-2793.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2781-2793
    • Myers, J.M.1    Myers, C.R.2
  • 22
    • 0032516752 scopus 로고    scopus 로고
    • Isolation and sequence of omcA, a gene encoding a decaheme outer membrane cytochrome c of Shewanella putrefaciens MR-1, and detection of omcA homologs in other strains of S. putrefaciens
    • Myers, J. M., and C. R. Myers. 1998. Isolation and sequence of omcA, a gene encoding a decaheme outer membrane cytochrome c of Shewanella putrefaciens MR-1, and detection of omcA homologs in other strains of S. putrefaciens. Biochim. Biophys. Acta 1373:237-251.
    • (1998) Biochim. Biophys. Acta , vol.1373 , pp. 237-251
    • Myers, J.M.1    Myers, C.R.2
  • 23
    • 0035166832 scopus 로고    scopus 로고
    • Role for outer membrane cytochromes OmcA and OmcB of Shewanella putrefaciens MR-1 in reduction of manganese dioxide
    • Myers, J. M., and C. R. Myers. 2001. Role for outer membrane cytochromes OmcA and OmcB of Shewanella putrefaciens MR-1 in reduction of manganese dioxide. Appl. Environ. Microbiol. 67:260-269.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 260-269
    • Myers, J.M.1    Myers, C.R.2
  • 24
    • 0033989646 scopus 로고    scopus 로고
    • Role of the tetraheme cytochrome CymA in anaerobic electron transport in cells of Shewanella putrefaciens MR-1 with normal levels of menaquinone
    • Myers, J. M., and C. R. Myers. 2000. Role of the tetraheme cytochrome CymA in anaerobic electron transport in cells of Shewanella putrefaciens MR-1 with normal levels of menaquinone. J. Bacteriol. 182:67-75.
    • (2000) J. Bacteriol. , vol.182 , pp. 67-75
    • Myers, J.M.1    Myers, C.R.2
  • 25
    • 0028132223 scopus 로고
    • Iron and manganese in anaerobic respiration: Environmental significance, physiology, and regulation
    • Nealson, K. H., and D. Saffarini. 1994. Iron and manganese in anaerobic respiration: environmental significance, physiology, and regulation. Annu. Rev. Microbiol. 48:311-343.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 311-343
    • Nealson, K.H.1    Saffarini, D.2
  • 27
    • 0041344634 scopus 로고    scopus 로고
    • Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: Expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates
    • Pitts, K. E., P. S. Dobbin, F. Reyes-Ramirez, A. J. Thomson, D. J. Richardson, and H. E. Seward. 2003. Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates. J. Biol. Chem. 278:27758-27765.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27758-27765
    • Pitts, K.E.1    Dobbin, P.S.2    Reyes-Ramirez, F.3    Thomson, A.J.4    Richardson, D.J.5    Seward, H.E.6
  • 28
    • 20544459308 scopus 로고    scopus 로고
    • High-throughput proteomics using Fourier transform ion cyclotron resonance mass spectrometry
    • Qian, W. J., D. G. Camp II, and R. D. Smith. 2004. High-throughput proteomics using Fourier transform ion cyclotron resonance mass spectrometry. Expert Rev. Proteomics 1:87-95.
    • (2004) Expert Rev. Proteomics , vol.1 , pp. 87-95
    • Qian, W.J.1    Camp II, D.G.2    Smith, R.D.3
  • 29
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. 2000. Bacterial respiration: a flexible process for a changing environment. Microbiology 146(Pt. 3):551-571.
    • (2000) Microbiology , vol.146 , Issue.PART 3 , pp. 551-571
    • Richardson, D.J.1
  • 30
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann, M. G., D. Moras, and K. W. Olsen. 1974. Chemical and biological evolution of nucleotide-binding protein. Nature 250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 31
    • 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
    • Seeliger, S., R. Cord-Ruwisch, and B. Schink. 1998. 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. 180:3686-3691.
    • (1998) J. Bacteriol. , vol.180 , pp. 3686-3691
    • Seeliger, S.1    Cord-Ruwisch, R.2    Schink, B.3
  • 33
    • 0021332775 scopus 로고
    • Characterization of the interaction of cytochrome c and mitochondrial ubiquinol-cytochrome c reductase
    • Speck, S. H., and E. Margoliash. 1984. Characterization of the interaction of cytochrome c and mitochondrial ubiquinol-cytochrome c reductase. J. Biol. Chem. 259:1064-1072.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1064-1072
    • Speck, S.H.1    Margoliash, E.2
  • 34
    • 0037154095 scopus 로고    scopus 로고
    • The inhibitory action of phospholamban involves stabilization of alpha-helices within the Ca-ATPase
    • Tatulian, S. A., B. Chen, J. Li, S. Negash, C. R. Middaugh, D. J. Bigelow, and T. C. Squier. 2002. The inhibitory action of phospholamban involves stabilization of alpha-helices within the Ca-ATPase. Biochemistry 41:741-751.
    • (2002) Biochemistry , vol.41 , pp. 741-751
    • Tatulian, S.A.1    Chen, B.2    Li, J.3    Negash, S.4    Middaugh, C.R.5    Bigelow, D.J.6    Squier, T.C.7
  • 35
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas, P. E., D. Ryan, and W. Levin. 1976. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 75:168-176.
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 36
    • 0036842435 scopus 로고    scopus 로고
    • Shewanella-the environmentally versatile genome
    • Tiedje, J. M. 2002. Shewanella-the environmentally versatile genome. Nat. Biotechnol. 20:1093-1094.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1093-1094
    • Tiedje, J.M.1
  • 37
    • 0036010279 scopus 로고    scopus 로고
    • Chromate reduction in Shewanella oneidemis MR-1 is an inducible process associated with anaerobic growth
    • Viamajala, S., B. M. Peyton, W. A. Apel, and J. N. Petersen. 2002. Chromate reduction in Shewanella oneidemis MR-1 is an inducible process associated with anaerobic growth. Biotechnol. Prog. 18:290-295.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 290-295
    • Viamajala, S.1    Peyton, B.M.2    Apel, W.A.3    Petersen, J.N.4
  • 38
    • 0037199162 scopus 로고    scopus 로고
    • Chromate/nitrite interactions in Shewanella oneidensis MR-1: Evidence for multiple hexavalent chromium [Cr(VI)] reduction mechanisms dependent on physiological growth conditions
    • Viamajala, S., B. M. Peyton, W. A. Apel, and J. N. Petersen. 2002. Chromate/nitrite interactions in Shewanella oneidensis MR-1: evidence for multiple hexavalent chromium [Cr(VI)] reduction mechanisms dependent on physiological growth conditions. Biotechnol. Bioeng. 78:770-778.
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 770-778
    • Viamajala, S.1    Peyton, B.M.2    Apel, W.A.3    Petersen, J.N.4
  • 39
    • 0042431786 scopus 로고    scopus 로고
    • Modeling chromate reduction in Shewanella oneidensis MR-1: Development of a novel dual-enzyme kinetic model
    • Viamajala, S., B. M. Peyton, and J. N. Petersen. 2003. Modeling chromate reduction in Shewanella oneidensis MR-1: development of a novel dual-enzyme kinetic model. Biotechnol. Bioeng. 83:790-797.
    • (2003) Biotechnol. Bioeng. , vol.83 , pp. 790-797
    • Viamajala, S.1    Peyton, B.M.2    Petersen, J.N.3
  • 40
    • 0343485086 scopus 로고    scopus 로고
    • Isolation of U(VI) reduction-deficient mutants of Shewanella putrefaciens
    • Wade, R., and T. J. DiChristina. 2000. Isolation of U(VI) reduction-deficient mutants of Shewanella putrefaciens. FEMS Microbiol. Lett. 184:143-148.
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 143-148
    • Wade, R.1    Dichristina, T.J.2
  • 41
    • 0034096598 scopus 로고    scopus 로고
    • Kinetics and mechanism of surface reaction of salicylate on alumina in colloidal aqueous suspension
    • Wang, Z., C. C. Ainsworth, D. M. Friedrich, P. L. Gassman, and A. G. Joly. 2000. Kinetics and mechanism of surface reaction of salicylate on alumina in colloidal aqueous suspension. Geochem. Cosmochim. 64:1159-1172.
    • (2000) Geochem. Cosmochim. , vol.64 , pp. 1159-1172
    • Wang, Z.1    Ainsworth, C.C.2    Friedrich, D.M.3    Gassman, P.L.4    Joly, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.