메뉴 건너뛰기




Volumn 13, Issue 4, 2009, Pages 436-442

Single molecule enzymology: Watching the reaction

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; ENZYME INHIBITOR;

EID: 84861854858     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2009.06.011     Document Type: Review
Times cited : (16)

References (51)
  • 1
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo C, Balci H, Ishitsuka Y, Buranachai C, Ha T. Advances in single-molecule fluorescence methods for molecular biology. Annu Rev Biochem 2008, 77:51-76.
    • (2008) Annu Rev Biochem , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 2
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy, optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman KC, Nagy A. Single-molecule force spectroscopy, optical tweezers, magnetic tweezers and atomic force microscopy. Nat Methods 2008, 5:491-505.
    • (2008) Nat Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 3
    • 48349090299 scopus 로고    scopus 로고
    • See me, feel me, methods to concurrently visualize and manipulate single DNA molecules and associated proteins
    • van Mameren J, Peterman EJG, Wuite GJL. See me, feel me, methods to concurrently visualize and manipulate single DNA molecules and associated proteins. Nucl Acids Res 2008, 36:4381-4389.
    • (2008) Nucl Acids Res , vol.36 , pp. 4381-4389
    • van Mameren, J.1    Peterman, E.J.G.2    Wuite, G.J.L.3
  • 4
    • 44449097780 scopus 로고    scopus 로고
    • Do-it-yourself guide, how to use the modern single-molecule toolkit
    • Walter NG, Huang C-Y, Manzo AJ, Sobhy MA. Do-it-yourself guide, how to use the modern single-molecule toolkit. Nat Methods 2008, 5:475-489.
    • (2008) Nat Methods , vol.5 , pp. 475-489
    • Walter, N.G.1    Huang, C.-Y.2    Manzo, A.J.3    Sobhy, M.A.4
  • 5
    • 50149109300 scopus 로고    scopus 로고
    • Single-molecule studies of RNA polymerase: motoring along
    • Herbert KM, Greenleaf WJ, Block SM. Single-molecule studies of RNA polymerase: motoring along. Annu Rev Biochem 2008, 77:149-176.
    • (2008) Annu Rev Biochem , vol.77 , pp. 149-176
    • Herbert, K.M.1    Greenleaf, W.J.2    Block, S.M.3
  • 6
    • 60349097663 scopus 로고    scopus 로고
    • Single-molecule observations of ribosome function
    • Blanchard SC. Single-molecule observations of ribosome function. Curr Opin Struct Biol 2009, 19:103-109.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 103-109
    • Blanchard, S.C.1
  • 7
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle AM. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu Rev Biophys 2008, 37:317-336.
    • (2008) Annu Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 8
    • 60749121148 scopus 로고    scopus 로고
    • Walking the walk, how kinesin and dynein coordinate their steps
    • Gennerich A, Vale RD. Walking the walk, how kinesin and dynein coordinate their steps. Curr Opin Cell Biol 2009, 21:59-67.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 59-67
    • Gennerich, A.1    Vale, R.D.2
  • 10
    • 35448981947 scopus 로고    scopus 로고
    • Stochastic inhibitor release and binding from single-enzyme molecules
    • Gorris HH, Rissin DM, Walt DR. Stochastic inhibitor release and binding from single-enzyme molecules. Proc Natl Acad Sci U S A 2007, 104:17680-17685.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17680-17685
    • Gorris, H.H.1    Rissin, D.M.2    Walt, D.R.3
  • 11
    • 20444373710 scopus 로고    scopus 로고
    • The structure of E. coli beta-galactosidase
    • Matthews BW. The structure of E. coli beta-galactosidase. C R Biologies 2005, 328:549-556.
    • (2005) C R Biologies , vol.328 , pp. 549-556
    • Matthews, B.W.1
  • 12
    • 42149136142 scopus 로고    scopus 로고
    • Distinct and long-lived activity states of single enzyme molecules
    • Rissin DM, Gorris HH, Walt DR. Distinct and long-lived activity states of single enzyme molecules. J Am Chem Soc 2008, 130:5349-5353.
    • (2008) J Am Chem Soc , vol.130 , pp. 5349-5353
    • Rissin, D.M.1    Gorris, H.H.2    Walt, D.R.3
  • 13
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy R, Hohng S, Ha T. A practical guide to single-molecule FRET. Nat Methods 2008, 5:507-516.
    • (2008) Nat Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 16
    • 34447628890 scopus 로고    scopus 로고
    • Coupling of rotation and catalysis in F1-ATPase revealed by single-molecule imaging and manipulation
    • Adachi K, Oiwa K, Nishizaka T, Furuike S, Noji H, Itoh H, Yoshida M, Kinosita K Jr. Coupling of rotation and catalysis in F1-ATPase revealed by single-molecule imaging and manipulation. Cell 2007, 130:309-321.
    • (2007) Cell , vol.130 , pp. 309-321
    • Adachi, K.1    Oiwa, K.2    Nishizaka, T.3    Furuike, S.4    Noji, H.5    Itoh, H.6    Yoshida, M.7    Kinosita Jr, K.8
  • 20
    • 57149107555 scopus 로고    scopus 로고
    • Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80- and 40- substep rotations
    • Masaike T, Koyama-Horibe F, Oiwa K, Yoshida M, Nishizaka T. Cooperative three-step motions in catalytic subunits of F1-ATPase correlate with 80- and 40- substep rotations. Nat Struct Mol Biol 2008, 15:1326-1333
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1326-1333
    • Masaike, T.1    Koyama-Horibe, F.2    Oiwa, K.3    Yoshida, M.4    Nishizaka, T.5
  • 23
    • 58149352850 scopus 로고    scopus 로고
    • Single molecule studies of homologous recombination
    • Finkelstein IJ, Greene EC. Single molecule studies of homologous recombination. Molecular BioSystems 2008, 4:1094-1104.
    • (2008) Molecular BioSystems , vol.4 , pp. 1094-1104
    • Finkelstein, I.J.1    Greene, E.C.2
  • 24
    • 34547877610 scopus 로고    scopus 로고
    • Fueling protein-DNA interactions inside porous nanocontainers
    • Cisse I, Okumus B, Joo C, Ha T Fueling protein-DNA interactions inside porous nanocontainers. Proc Natl Acad Sci U S A 2007, 104:12646-12650.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12646-12650
    • Cisse, I.1    Okumus, B.2    Joo, C.3    Ha, T.4
  • 27
    • 35348987552 scopus 로고    scopus 로고
    • Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA
    • Farbman ME, Gershenson A, Licht S. Single-molecule analysis of nucleotide-dependent substrate binding by the protein unfoldase ClpA. J Am Chem Soc 2007, 129:12378-12379.
    • (2007) J Am Chem Soc , vol.129 , pp. 12378-12379
    • Farbman, M.E.1    Gershenson, A.2    Licht, S.3
  • 28
    • 58149159717 scopus 로고    scopus 로고
    • Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA
    • Farbman ME, Gershenson A, Licht S. Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA. Biochemistry 2008, 47:13497-13505.
    • (2008) Biochemistry , vol.47 , pp. 13497-13505
    • Farbman, M.E.1    Gershenson, A.2    Licht, S.3
  • 29
    • 3042640723 scopus 로고    scopus 로고
    • Rotation of F1-ATPase How an ATP-driven molecular machine may work
    • Kinosita K, Adachi K, Itoh H. Rotation of F1-ATPase. How an ATP-driven molecular machine may work. Annu Rev Biophys Biomol Struct 2004, 33:245-268.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 245-268
    • Kinosita, K.1    Adachi, K.2    Itoh, H.3
  • 30
    • 48249108462 scopus 로고    scopus 로고
    • Unique rotary ATP synthase and its biological diversity
    • von Ballmoos C, Cook GM, Dimroth P. Unique rotary ATP synthase and its biological diversity. Annu Rev Biophys 2008, 37:43-64.
    • (2008) Annu Rev Biophys , vol.37 , pp. 43-64
    • von Ballmoos, C.1    Cook, G.M.2    Dimroth, P.3
  • 31
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K Jr. Direct observation of the rotation of F1-ATPase. Nature 1997, 386:299-302.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr, K.4
  • 32
    • 0742270602 scopus 로고    scopus 로고
    • Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation
    • Nishizaka T, Oiwa K, Noji H, Kimura S, Muneyuki E, Yoshida M, Kinosita K. Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation. Nat Struct Mol Biol 2004, 11:142-148.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 142-148
    • Nishizaka, T.1    Oiwa, K.2    Noji, H.3    Kimura, S.4    Muneyuki, E.5    Yoshida, M.6    Kinosita, K.7
  • 34
    • 34347226731 scopus 로고    scopus 로고
    • Ground state structure of F1-ATPase from bovine heart mitochondria at 1 9 A resolution
    • Bowler MW, Montgomery MG, Leslie AGW, Walker JE. Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution. J Biol Chem 2007, 282:14238-14242.
    • (2007) J Biol Chem , vol.282 , pp. 14238-14242
    • Bowler, M.W.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 35
    • 0032547899 scopus 로고    scopus 로고
    • Energy transduction in the F1 motor of ATP synthase
    • Wang H, Oster G. Energy transduction in the F1 motor of ATP synthase. Nature 1998, 396:279-282.
    • (1998) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 38
    • 56449114709 scopus 로고    scopus 로고
    • Slide into action Dynamic shuttling of HIV reverse transcriptase on nucleic acid substrates
    • Liu S, Abbondanzieri EA, Rausch JW, Grice SFJL, Zhuang X. Slide into action. Dynamic shuttling of HIV reverse transcriptase on nucleic acid substrates. Science 2008, 322:1092-1097.
    • (2008) Science , vol.322 , pp. 1092-1097
    • Liu, S.1    Abbondanzieri, E.A.2    Rausch, J.W.3    Grice Sfjl4    Zhuang, X.5
  • 39
    • 58149133507 scopus 로고    scopus 로고
    • Structure and function of HIV-1 reverse transcriptase Molecular mechanisms of polymerization and inhibition
    • Sarafianos SG, Marchand B, Das K, Himmel DM, Parniak MA, Hughes SH, Arnold E. Structure and function of HIV-1 reverse transcriptase. Molecular mechanisms of polymerization and inhibition. J Mol Biol 2009, 385:693-713.
    • (2009) J Mol Biol , vol.385 , pp. 693-713
    • Sarafianos, S.G.1    Marchand, B.2    Das, K.3    Himmel, D.M.4    Parniak, M.A.5    Hughes, S.H.6    Arnold, E.7
  • 40
    • 67650227918 scopus 로고    scopus 로고
    • Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity Insights into phosphatidylcholine activation and surface dilution inhibition
    • Pu M, Fang X, Redfield AG, Gershenson A, Roberts MF. Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity. Insights into phosphatidylcholine activation and surface dilution inhibition. J Biol Chem 2009, 284:16099-16107.
    • (2009) J Biol Chem , vol.284 , pp. 16099-16107
    • Pu, M.1    Fang, X.2    Redfield, A.G.3    Gershenson, A.4    Roberts, M.F.5
  • 41
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • Rhoades E, Ramlall TF, Webb WW, Eliezer D. Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy. Biophys J 2006, 90:4692-4700.
    • (2006) Biophys J , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 42
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles
    • Rusu L, Gambhir A, McLaughlin S, Rädler J. Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles. Biophys J 2004, 87:1044-1053.
    • (2004) Biophys J , vol.87 , pp. 1044-1053
    • Rusu, L.1    Gambhir, A.2    McLaughlin, S.3    Rädler, J.4
  • 43
    • 0033552653 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of the hydrophobic interactions of protein 4 1 with phosphatidyl serine liposomes
    • Takakuwa Y, Pack CG, An XL, Manno S, Ito E, Kinjo M. Fluorescence correlation spectroscopy analysis of the hydrophobic interactions of protein 4.1 with phosphatidyl serine liposomes. Biophys Chem 1999, 82:149-155.
    • (1999) Biophys Chem , vol.82 , pp. 149-155
    • Takakuwa, Y.1    Pack, C.G.2    An, X.L.3    Manno, S.4    Ito, E.5    Kinjo, M.6
  • 44
    • 60849098172 scopus 로고    scopus 로고
    • Fluorescence singlemolecule study of cobra phospholipase A2 action on a supported gel-phase lipid bilayer
    • Chiu C-R, Huang W-N, Wu W-G, Yang T-S. Fluorescence singlemolecule study of cobra phospholipase A2 action on a supported gel-phase lipid bilayer. Chemphyschem 2009, 10:549-558.
    • (2009) Chemphyschem , vol.10 , pp. 549-558
    • Chiu, C.-R.1    Huang, W.-N.2    Wu, W.-G.3    Yang, T.-S.4
  • 46
    • 34547824727 scopus 로고    scopus 로고
    • Tracking single lipase molecules on a trimyristin substrate surface using quantum dots
    • Sonesson AW, Elofsson UM, Callisen TH, Brismar H. Tracking single lipase molecules on a trimyristin substrate surface using quantum dots. Langmuir 2007, 23:8352-8356.
    • (2007) Langmuir , vol.23 , pp. 8352-8356
    • Sonesson, A.W.1    Elofsson, U.M.2    Callisen, T.H.3    Brismar, H.4
  • 47
    • 39449139613 scopus 로고    scopus 로고
    • Lipid diffusion from single molecules of a labeled protein undergoing dynamic association with giant unilamellar vesicles and supported bilayers
    • Sharonov A, Bandichhor R, Burgess K, Petrescu AD, Schroeder F, Kier AB, Hochstrasser RM. Lipid diffusion from single molecules of a labeled protein undergoing dynamic association with giant unilamellar vesicles and supported bilayers. Langmuir 2008, 24:844-850.
    • (2008) Langmuir , vol.24 , pp. 844-850
    • Sharonov, A.1    Bandichhor, R.2    Burgess, K.3    Petrescu, A.D.4    Schroeder, F.5    Kier, A.B.6    Hochstrasser, R.M.7
  • 48
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain Newinsights into the membrane docking reaction
    • Knight JD, Falke JJ. Single-molecule fluorescence studies of a PH domain. Newinsights into the membrane docking reaction. Biophys J 2009, 96:566-582.
    • (2009) Biophys J , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 49
    • 52649162907 scopus 로고    scopus 로고
    • DNA curtains and nanoscale curtain rods High-throughput tools for single molecule imaging
    • Fazio T, Visnapuu M-L, Wind S, Greene EC. DNA curtains and nanoscale curtain rods. High-throughput tools for single molecule imaging. Langmuir 2008, 24:10524-10531.
    • (2008) Langmuir , vol.24 , pp. 10524-10531
    • Fazio, T.1    Visnapuu, M.-L.2    Wind, S.3    Greene, E.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.