메뉴 건너뛰기




Volumn 119, Issue 20, 2015, Pages 6129-6143

Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINS; CELLULOSE; CHAINS; COPOLYMERS; CRYSTALLINE MATERIALS; ENZYMES; FREE ENERGY; GLUCOSE; HYDROLASES; OLIGOMERS; ORGANIC POLYMERS;

EID: 84930227196     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b00778     Document Type: Article
Times cited : (94)

References (101)
  • 7
    • 77950948151 scopus 로고    scopus 로고
    • Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61: Structure and Function of a Large, Enigmatic Family
    • Harris, P. V.; Welner, D.; McFarland, K. C.; Re, E.; Poulsen, J. C. N.; Brown, K.; Salbo, R.; Ding, H. S.; Vlasenko, E.; Merino, S. Stimulation of Lignocellulosic Biomass Hydrolysis by Proteins of Glycoside Hydrolase Family 61: Structure and Function of a Large, Enigmatic Family Biochemistry 2010, 49, 3305-3316
    • (2010) Biochemistry , vol.49 , pp. 3305-3316
    • Harris, P.V.1    Welner, D.2    Mcfarland, K.C.3    Re, E.4    Poulsen, J.C.N.5    Brown, K.6    Salbo, R.7    Ding, H.S.8    Vlasenko, E.9    Merino, S.10
  • 8
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose Dehydrogenase and a Copper-Dependent Polysaccharide Monooxygenase Potentiate Cellulose Degradation by Neurospora crassa
    • Phillips, C. M.; Beeson, W. T.; Cate, J. H.; Marletta, M. A. Cellobiose Dehydrogenase and a Copper-Dependent Polysaccharide Monooxygenase Potentiate Cellulose Degradation by Neurospora crassa ACS Chem. Biol. 2011, 6, 1399-1406
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 9
    • 84855912007 scopus 로고    scopus 로고
    • Oxidative Cleavage of Cellulose by Fungal Copper-Dependent Polysaccharide Monooxygenases
    • Beeson, W. T.; Phillips, C. M.; Cate, J. H. D.; Marletta, M. A. Oxidative Cleavage of Cellulose by Fungal Copper-Dependent Polysaccharide Monooxygenases J. Am. Chem. Soc. 2012, 134, 890-892
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 890-892
    • Beeson, W.T.1    Phillips, C.M.2    Cate, J.H.D.3    Marletta, M.A.4
  • 12
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive Cellulose Depolymerization by the Enzymes Cellobiose Dehydrogenase and Glycoside Hydrolase 61
    • Langston, J. A.; Shaghasi, T.; Abbate, E.; Xu, F.; Vlasenko, E.; Sweeney, M. D. Oxidoreductive Cellulose Depolymerization by the Enzymes Cellobiose Dehydrogenase and Glycoside Hydrolase 61 Appl. Environ. Microbiol. 2011, 77, 7007-7015
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 14
    • 52049106382 scopus 로고    scopus 로고
    • The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B From Hypocrea jecorina, at 1.6Å Resolution
    • Karkehabadi, S.; Hansson, H.; Kim, S.; Piens, K.; Mitchinson, C.; Sandgren, M. The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B From Hypocrea jecorina, at 1.6Å Resolution J. Mol. Biol. 2008, 383, 144-154
    • (2008) J. Mol. Biol. , vol.383 , pp. 144-154
    • Karkehabadi, S.1    Hansson, H.2    Kim, S.3    Piens, K.4    Mitchinson, C.5    Sandgren, M.6
  • 15
    • 84891926133 scopus 로고    scopus 로고
    • Quantum Mechanical Calculations Suggest That Lytic Polysaccharide Monooxygenases Use a Copper-Oxyl, Oxygen-Rebound Mechanism
    • Kim, S.; Stahlberg, J.; Sandgren, M.; Paton, R. S.; Beckham, G. T. Quantum Mechanical Calculations Suggest That Lytic Polysaccharide Monooxygenases Use a Copper-Oxyl, Oxygen-Rebound Mechanism Proc. Natl. Acad. Sci. U.S.A. 2014, 111, 149-154
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 149-154
    • Kim, S.1    Stahlberg, J.2    Sandgren, M.3    Paton, R.S.4    Beckham, G.T.5
  • 16
    • 84877151161 scopus 로고    scopus 로고
    • Crystal Structure and Computational Characterization of the Lytic Polysaccharide Monooxygenase GH61D From the Basidiomycota Fungus Phanerochaete chrysosporium
    • Wu, M.; Beckham, G. T.; Larsson, A. M.; Ishida, T.; Kim, S.; Payne, C. M.; Himmel, M. E.; Crowley, M. F.; Horn, S. J.; Westereng, B. Crystal Structure and Computational Characterization of the Lytic Polysaccharide Monooxygenase GH61D From the Basidiomycota Fungus Phanerochaete chrysosporium J. Biol. Chem. 2013, 288, 12828-12839
    • (2013) J. Biol. Chem. , vol.288 , pp. 12828-12839
    • Wu, M.1    Beckham, G.T.2    Larsson, A.M.3    Ishida, T.4    Kim, S.5    Payne, C.M.6    Himmel, M.E.7    Crowley, M.F.8    Horn, S.J.9    Westereng, B.10
  • 18
    • 84897113991 scopus 로고    scopus 로고
    • Discovery and Characterization of a New Family of Lytic Polysaccharide Monooxygenases
    • Hemsworth, G. R.; Henrissat, B.; Davies, G. J.; Walton, P. H. Discovery and Characterization of a New Family of Lytic Polysaccharide Monooxygenases Nat. Chem. Biol. 2014, 10, 122-126
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 122-126
    • Hemsworth, G.R.1    Henrissat, B.2    Davies, G.J.3    Walton, P.H.4
  • 20
    • 84869205445 scopus 로고    scopus 로고
    • NMR Structure of a Lytic Polysaccharide Monooxygenase Provides Insight Into Copper Binding, Protein Dynamics, and Substrate Interactions
    • Aachmann, F. L.; Sørlie, M.; Skjak-Bræk, G.; Eijsink, V. G. H.; Vaaje-Kolstad, G. NMR Structure of a Lytic Polysaccharide Monooxygenase Provides Insight Into Copper Binding, Protein Dynamics, and Substrate Interactions Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 18779-18784
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18779-18784
    • Aachmann, F.L.1    Sørlie, M.2    Skjak-Bræk, G.3    Eijsink, V.G.H.4    Vaaje-Kolstad, G.5
  • 21
  • 24
    • 84919820322 scopus 로고    scopus 로고
    • Cellulose Surface Degradation by a Lytic Polysaccharide Monooxygenase and Its Effect on Cellulase Hydrolytic Efficiency
    • Eibinger, M.; Ganner, T.; Bubner, P.; Rosker, S.; Kracher, D.; Haltrich, D.; Ludwig, R.; Plank, H.; Nidetzky, B. Cellulose Surface Degradation by a Lytic Polysaccharide Monooxygenase and Its Effect on Cellulase Hydrolytic Efficiency J. Biol. Chem. 2014, 289, 35929-35938
    • (2014) J. Biol. Chem. , vol.289 , pp. 35929-35938
    • Eibinger, M.1    Ganner, T.2    Bubner, P.3    Rosker, S.4    Kracher, D.5    Haltrich, D.6    Ludwig, R.7    Plank, H.8    Nidetzky, B.9
  • 25
    • 84892745213 scopus 로고    scopus 로고
    • Determinants of Regioselective Hydroxylation in the Fungal Polysaccharide Monooxygenases
    • Vu, V. V.; Beeson, W. T.; Phillips, C. M.; Cate, J. H. D.; Marletta, M. A. Determinants of Regioselective Hydroxylation in the Fungal Polysaccharide Monooxygenases J. Am. Chem. Soc. 2014, 136, 562-565
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 562-565
    • Vu, V.V.1    Beeson, W.T.2    Phillips, C.M.3    Cate, J.H.D.4    Marletta, M.A.5
  • 26
    • 0000270016 scopus 로고
    • The Lactone-Acid-Salt Equilibria for D-Glucono-lactone and the Hydrolysis Kinetics for This Lactone
    • Sawyer, D. T.; Bagger, J. B. The Lactone-Acid-Salt Equilibria for D-Glucono-lactone and the Hydrolysis Kinetics for This Lactone J. Am. Chem. Soc. 1959, 81, 5302-5306
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 5302-5306
    • Sawyer, D.T.1    Bagger, J.B.2
  • 27
    • 0037036704 scopus 로고    scopus 로고
    • Crystal Structure and Hydrogen-Bonding System in Cellulose Iβ From Synchrotron X-Ray and Neutron Fiber Diffraction
    • Nishiyama, Y.; Langan, P.; Chanzy, H. Crystal Structure and Hydrogen-Bonding System in Cellulose Iβ From Synchrotron X-Ray and Neutron Fiber Diffraction J. Am. Chem. Soc. 2002, 124, 9074-9082
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9074-9082
    • Nishiyama, Y.1    Langan, P.2    Chanzy, H.3
  • 28
    • 0344443362 scopus 로고    scopus 로고
    • Crystal Structure and Hydrogen Bonding System in Cellulose Iα From Synchrotron X-Ray and Neutron Fiber Diffraction
    • Nishiyama, Y.; Sugiyama, J.; Chanzy, H.; Langan, P. Crystal Structure and Hydrogen Bonding System in Cellulose Iα From Synchrotron X-Ray and Neutron Fiber Diffraction J. Am. Chem. Soc. 2003, 125, 14300-14306
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14300-14306
    • Nishiyama, Y.1    Sugiyama, J.2    Chanzy, H.3    Langan, P.4
  • 31
    • 79953780010 scopus 로고    scopus 로고
    • Analysis of Twisting of Cellulose Nanofibrils in Atomistic Molecular Dynamics Simulations
    • Paavilainen, S.; Róg, T.; Vattulainen, I. Analysis of Twisting of Cellulose Nanofibrils in Atomistic Molecular Dynamics Simulations J. Phys. Chem. B 2011, 115, 3747-3755
    • (2011) J. Phys. Chem. B , vol.115 , pp. 3747-3755
    • Paavilainen, S.1    Róg, T.2    Vattulainen, I.3
  • 32
    • 84862173322 scopus 로고    scopus 로고
    • Production and Effect of Aldonic Acids During Enzymatic Hydrolysis of Lignocellulose at High Dry Matter Content
    • Cannella, D.; Hsieh, C.-W. C.; Felby, C.; Jørgensen, H. Production and Effect of Aldonic Acids During Enzymatic Hydrolysis of Lignocellulose at High Dry Matter Content Biotechnol. Biofuels 2012, 5, 26
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 26
    • Cannella, D.1    Hsieh, C.-W.C.2    Felby, C.3    Jørgensen, H.4
  • 33
    • 84888051667 scopus 로고    scopus 로고
    • Do New Cellulolytic Enzyme Preparations Affect the Industrial Strategies for High Solids Lignocellulosic Ethanol Production?
    • Cannella, D.; Jørgensen, H. Do New Cellulolytic Enzyme Preparations Affect the Industrial Strategies for High Solids Lignocellulosic Ethanol Production? Biotechnol. Bioeng. 2014, 111, 59-68
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 59-68
    • Cannella, D.1    Jørgensen, H.2
  • 35
    • 79953781576 scopus 로고    scopus 로고
    • Molecular-Level Origins of Biomass Recalcitrance: Decrystallization Free Energies for Four Common Cellulose Polymorphs
    • Beckham, G. T.; Matthews, J. F.; Peters, B.; Bomble, Y. J.; Himmel, M. E.; Crowley, M. F. Molecular-Level Origins of Biomass Recalcitrance: Decrystallization Free Energies for Four Common Cellulose Polymorphs J. Phys. Chem. B 2011, 115, 4118-4127
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4118-4127
    • Beckham, G.T.1    Matthews, J.F.2    Peters, B.3    Bomble, Y.J.4    Himmel, M.E.5    Crowley, M.F.6
  • 36
    • 79954528805 scopus 로고    scopus 로고
    • Examination of the α-chitin Structure and Decrystallization Thermodynamics at the Nanoscale
    • Beckham, G. T.; Crowley, M. F. Examination of the α-chitin Structure and Decrystallization Thermodynamics at the Nanoscale J. Phys. Chem. B 2011, 115, 4516-4522
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4516-4522
    • Beckham, G.T.1    Crowley, M.F.2
  • 37
    • 79960171999 scopus 로고    scopus 로고
    • Decrystallization of Oligosaccharides From the Cellulose Iβ Surface With Molecular Simulation
    • Payne, C. M.; Himmel, M. E.; Crowley, M. F.; Beckham, G. T. Decrystallization of Oligosaccharides From the Cellulose Iβ Surface With Molecular Simulation J. Phys. Chem. Lett. 2011, 2, 1546-1550
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 1546-1550
    • Payne, C.M.1    Himmel, M.E.2    Crowley, M.F.3    Beckham, G.T.4
  • 38
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes
    • Ryckaert, J.-P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 39
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N log(N) Methods for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. G. Particle Mesh Ewald: An N log(N) Methods for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.G.3
  • 45
  • 49
    • 0001538909 scopus 로고
    • Canonical Dynamics: Equilibrium Phase-Space Distributions
    • Hoover, W. G. Canonical Dynamics: Equilibrium Phase-Space Distributions Phys. Rev. A 1985, 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 50
    • 34547809547 scopus 로고
    • A Unified Formulation of the Constant Temperature Molecular Dynamics Methods
    • Nosé, S. A Unified Formulation of the Constant Temperature Molecular Dynamics Methods J. Chem. Phys. 1984, 81, 511-519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nosé, S.1
  • 52
    • 48749137581 scopus 로고
    • Stochastic Boundary Conditions for Molecular Dynamics Simulations of ST2 Water
    • Brünger, A. T.; Brooks, C. L., III; Karplus, M. Stochastic Boundary Conditions for Molecular Dynamics Simulations of ST2 Water Chem. Phys. Lett. 1984, 105, 495-498
    • (1984) Chem. Phys. Lett. , vol.105 , pp. 495-498
    • Brünger, A.T.1    Brooks, C.L.2    Karplus, M.3
  • 53
    • 0037157693 scopus 로고    scopus 로고
    • A High-Performance Parallel-Generalized Born Implementation Enabled by Tabulated Interaction Rescaling
    • Lee, M. S.; Salsbury, F. R.; Brooks, C. L. A High-Performance Parallel-Generalized Born Implementation Enabled by Tabulated Interaction Rescaling J. Chem. Phys. 2002, 116, 10606-10614
    • (2002) J. Chem. Phys. , vol.116 , pp. 10606-10614
    • Lee, M.S.1    Salsbury, F.R.2    Brooks, C.L.3
  • 54
    • 33645703426 scopus 로고    scopus 로고
    • Balancing an Accurate Representation of the Molecular Surface in Generalized Born Formalisms With Integrator Stability in Molecular Dynamics Simulations
    • Chocholoušová, J.; Feig, M. Balancing an Accurate Representation of the Molecular Surface in Generalized Born Formalisms With Integrator Stability in Molecular Dynamics Simulations J. Comput. Chem. 2006, 27, 719-729
    • (2006) J. Comput. Chem. , vol.27 , pp. 719-729
    • Chocholoušová, J.1    Feig, M.2
  • 55
    • 84892868149 scopus 로고    scopus 로고
    • New Faster CHARMM Molecular Dynamics Engine
    • Hynninen, A. P.; Crowley, M. F. New Faster CHARMM Molecular Dynamics Engine J. Comput. Chem. 2014, 35, 406-413
    • (2014) J. Comput. Chem. , vol.35 , pp. 406-413
    • Hynninen, A.P.1    Crowley, M.F.2
  • 56
  • 57
    • 0032080053 scopus 로고    scopus 로고
    • Calculations on Folding of Segment B1 of Streptococcal Protein G
    • Sheinerman, F. B.; Brooks, C. L., III. Calculations on Folding of Segment B1 of Streptococcal Protein G J. Mol. Biol. 1998, 278, 439-456
    • (1998) J. Mol. Biol. , vol.278 , pp. 439-456
    • Sheinerman, F.B.1    Brooks, C.L.2
  • 58
    • 84889585833 scopus 로고    scopus 로고
    • Using Collective Variables to Drive Molecular Dynamics Simulations
    • Fiorin, G.; Klein, M. L.; Hénin, J. Using Collective Variables to Drive Molecular Dynamics Simulations Mol. Phys. 2013, 111, 3345-3362
    • (2013) Mol. Phys. , vol.111 , pp. 3345-3362
    • Fiorin, G.1    Klein, M.L.2    Hénin, J.3
  • 60
    • 84986519238 scopus 로고
    • The Weighted Histogram Analysis Method for Free-Energy Calculations on Biomolecules. I. The Method
    • Kumar, S.; Bouzida, D.; Swendsen, R. H.; Kollman, P. A.; Rosenberg, J. M. The Weighted Histogram Analysis Method for Free-Energy Calculations on Biomolecules. I. The Method J. Comput. Chem. 1992, 13, 1011-1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 61
    • 78651282170 scopus 로고    scopus 로고
    • G-wham-A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates
    • Hub, J. S.; de Groot, B. L.; van der Spoel, D. g-wham-A Free Weighted Histogram Analysis Implementation Including Robust Error and Autocorrelation Estimates J. Chem. Theory Comput. 2010, 6, 3713-3720
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 3713-3720
    • Hub, J.S.1    De Groot, B.L.2    Van Der Spoel, D.3
  • 62
    • 33646471468 scopus 로고
    • Statistical Mechanics of Fluid Mixtures
    • Kirkwood, J. G. Statistical Mechanics of Fluid Mixtures J. Chem. Phys. 1935, 3, 300-313
    • (1935) J. Chem. Phys. , vol.3 , pp. 300-313
    • Kirkwood, J.G.1
  • 63
    • 7044239742 scopus 로고
    • Free-Energy Calculations - Applications to Chemical and Biochemical Phenomena
    • Kollman, P. Free-Energy Calculations-Applications to Chemical and Biochemical Phenomena Chem. Rev. 1993, 93, 2395-2417
    • (1993) Chem. Rev. , vol.93 , pp. 2395-2417
    • Kollman, P.1
  • 64
    • 0033199581 scopus 로고    scopus 로고
    • Crystallographic Evidence for Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase Cel6A From Trichoderma reesei
    • Zou, J.; Kleywegt, G. J.; Stahlberg, J.; Driguez, H.; Nerinckx, W.; Claeyssens, M.; Koivula, A.; Teeri, T. T.; Jones, T. A. Crystallographic Evidence for Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase Cel6A From Trichoderma reesei Structure 1999, 7, 1035-1045
    • (1999) Structure , vol.7 , pp. 1035-1045
    • Zou, J.1    Kleywegt, G.J.2    Stahlberg, J.3    Driguez, H.4    Nerinckx, W.5    Claeyssens, M.6    Koivula, A.7    Teeri, T.T.8    Jones, T.A.9
  • 65
    • 0345676498 scopus 로고    scopus 로고
    • High-Resolution Crystal Structures Reveal How a Cellulose Chain Is Bound in the 50 Angstrom Long Tunnel of Cellobiohydrolase I From Trichoderma reesei
    • Divne, C.; Stahlberg, J.; Teeri, T. T.; Jones, T. A. High-Resolution Crystal Structures Reveal How a Cellulose Chain Is Bound in the 50 Angstrom Long Tunnel of Cellobiohydrolase I From Trichoderma reesei J. Mol. Biol. 1998, 275, 309-325
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 67
    • 36449003554 scopus 로고
    • Constant Pressure Molecular Dynamics Algorithms
    • Martyna, G. J.; Tobias, D. J.; Klein, M. L. Constant Pressure Molecular Dynamics Algorithms J. Chem. Phys. 1994, 101, 4177-4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 68
    • 36449007836 scopus 로고
    • Constant Pressure Molecular Dynamics Simulation: The Langevin Piston Method
    • Feller, S. E.; Zhang, Y.; Pastor, R. W.; Brooks, B. R. Constant Pressure Molecular Dynamics Simulation: The Langevin Piston Method J. Chem. Phys. 1995, 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 69
    • 58149147138 scopus 로고    scopus 로고
    • Single Mutation Induced H3N2 Hemagglutinin Antibody Neutralization: A Free Energy Perturbation Study
    • Zhou, R.; Das, P.; Royyuru, A. K. Single Mutation Induced H3N2 Hemagglutinin Antibody Neutralization: A Free Energy Perturbation Study J. Phys. Chem. B 2008, 112, 15813-15820
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15813-15820
    • Zhou, R.1    Das, P.2    Royyuru, A.K.3
  • 70
    • 77955577540 scopus 로고    scopus 로고
    • Good Practices in Free-energy Calculations
    • Pohorille, A.; Jarzynski, C.; Chipot, C. Good Practices in Free-energy Calculations J. Phys. Chem. B 2010, 114, 10235-10253
    • (2010) J. Phys. Chem. B , vol.114 , pp. 10235-10253
    • Pohorille, A.1    Jarzynski, C.2    Chipot, C.3
  • 71
    • 80053211021 scopus 로고    scopus 로고
    • Soft-Core Potentials in Thermodynamic Integration: Comparing One- and Two-Step Transformations
    • Steinbrecher, T.; Joung, I.; Case, D. A. Soft-Core Potentials in Thermodynamic Integration: Comparing One- and Two-Step Transformations J. Comput. Chem. 2011, 32, 3253-3263
    • (2011) J. Comput. Chem. , vol.32 , pp. 3253-3263
    • Steinbrecher, T.1    Joung, I.2    Case, D.A.3
  • 72
    • 1842692143 scopus 로고
    • General Definition of Ring Puckering Coordinates
    • Cremer, D.; Pople, J. A. General Definition of Ring Puckering Coordinates J. Am. Chem. Soc. 1975, 97, 1354-1358
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 1354-1358
    • Cremer, D.1    Pople, J.A.2
  • 73
    • 34250866873 scopus 로고    scopus 로고
    • Puckering Coordinates of Monocyclic Rings by Triangular Decomposition
    • Hill, A. D.; Reilly, P. J. Puckering Coordinates of Monocyclic Rings by Triangular Decomposition J. Chem. Inf. Model. 2007, 47, 1031-1035
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 1031-1035
    • Hill, A.D.1    Reilly, P.J.2
  • 74
    • 0001226736 scopus 로고
    • Conformational Studies on Aldonolactones by n.m.r. Spectroscopy. Conformations of D-Glucono-1,5-Lactone and D-Mannono-1,5-Lactone in Solution
    • Waaszek, Z.; Horton, D.; Ekiel, I. Conformational Studies on Aldonolactones by n.m.r. Spectroscopy. Conformations of D-Glucono-1,5-Lactone and D-Mannono-1,5-Lactone in Solution Carbohydr. Res. 1982, 106, 193-201
    • (1982) Carbohydr. Res. , vol.106 , pp. 193-201
    • Waaszek, Z.1    Horton, D.2    Ekiel, I.3
  • 75
    • 0141508976 scopus 로고    scopus 로고
    • Highly Diastereoselective Hydrogenations Leading to β-hydroxy-lactones in Hydroxy-Protected Form. A Modified View of-lactone Conformations
    • Brandänge, S.; Färnbäck, M.; Leijonmarck, H.; Sundin, A. Highly Diastereoselective Hydrogenations Leading to β-hydroxy -lactones in Hydroxy-Protected Form. A Modified View of lactone Conformations J. Am. Chem. Soc. 2003, 125, 11942-11955
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11942-11955
    • Brandänge, S.1    Färnbäck, M.2    Leijonmarck, H.3    Sundin, A.4
  • 76
    • 84987005648 scopus 로고
    • Correlation of Molecular Mechanics and NMR Data: Conformation and Configuration of the Meerwein Lactones
    • Stanley, J.; Matallana, A.; Kingsbury, C. A. Correlation of Molecular Mechanics and NMR Data: Conformation and Configuration of the Meerwein Lactones J. Phys. Org. Chem. 1990, 3, 419-427
    • (1990) J. Phys. Org. Chem. , vol.3 , pp. 419-427
    • Stanley, J.1    Matallana, A.2    Kingsbury, C.A.3
  • 77
    • 84871874790 scopus 로고    scopus 로고
    • Cello-Oligosaccharide Oxidation Reveals Differences Between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina
    • Bey, M.; Zhou, S.; Poidevin, L.; Henrissat, B.; Coutinho, P. M.; Berrin, J.-G.; Sigoillot, J.-C. Cello-Oligosaccharide Oxidation Reveals Differences Between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina Appl. Environ. Microbiol. 2013, 79, 488-496
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 488-496
    • Bey, M.1    Zhou, S.2    Poidevin, L.3    Henrissat, B.4    Coutinho, P.M.5    Berrin, J.-G.6    Sigoillot, J.-C.7
  • 78
    • 84878892982 scopus 로고    scopus 로고
    • Fungal Cellulases and Complexed Cellulosomal Enzymes Exhibit Synergistic Mechanisms in Cellulose Deconstruction
    • Resch, M. G.; Donohoe, B. S.; Baker, J. O.; Decker, S. R.; Bayer, E. A.; Beckham, G. T.; Himmel, M. E. Fungal Cellulases and Complexed Cellulosomal Enzymes Exhibit Synergistic Mechanisms in Cellulose Deconstruction Energy Environ. Sci. 2013, 6, 1858-1867
    • (2013) Energy Environ. Sci. , vol.6 , pp. 1858-1867
    • Resch, M.G.1    Donohoe, B.S.2    Baker, J.O.3    Decker, S.R.4    Bayer, E.A.5    Beckham, G.T.6    Himmel, M.E.7
  • 79
    • 84903464098 scopus 로고    scopus 로고
    • Integration of Bacterial Lytic Polysaccharide Monooxygenases Into Designer Cellulosomes Promotes Enhanced Cellulose Degradation
    • Arfi, Y.; Shamshoum, M.; Rogachev, I.; Peleg, Y.; Bayer, E. A. Integration of Bacterial Lytic Polysaccharide Monooxygenases Into Designer Cellulosomes Promotes Enhanced Cellulose Degradation Proc. Natl. Acad. Sci. U.S.A. 2014, 111, 9109-9114
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 9109-9114
    • Arfi, Y.1    Shamshoum, M.2    Rogachev, I.3    Peleg, Y.4    Bayer, E.A.5
  • 80
    • 84865224370 scopus 로고    scopus 로고
    • Endo-Exo Synergism in Cellulose Hydrolysis Revisited
    • Jalak, J.; Kurašin, M.; Teugjas, H.; Väljamäe, P. Endo-Exo Synergism in Cellulose Hydrolysis Revisited J. Biol. Chem. 2012, 287, 28802-28815
    • (2012) J. Biol. Chem. , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurašin, M.2    Teugjas, H.3    Väljamäe, P.4
  • 83
    • 79954418588 scopus 로고    scopus 로고
    • Applications of Computational Science for Understanding Enzymatic Deconstruction of Cellulose
    • Beckham, G. T.; Bomble, Y. J.; Bayer, E. A.; Himmel, M. E.; Crowley, M. F. Applications of Computational Science for Understanding Enzymatic Deconstruction of Cellulose Curr. Opin. Biotechnol. 2011, 22, 231-238
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 231-238
    • Beckham, G.T.1    Bomble, Y.J.2    Bayer, E.A.3    Himmel, M.E.4    Crowley, M.F.5
  • 84
    • 84890685861 scopus 로고    scopus 로고
    • Glycoside Hydrolase Processivity Is Directly Related to Oligosaccharide Binding Free Energy
    • Payne, C. M.; Jiang, W.; Shirts, M. R.; Himmel, M. E.; Crowley, M. F.; Beckham, G. T. Glycoside Hydrolase Processivity Is Directly Related to Oligosaccharide Binding Free Energy J. Am. Chem. Soc. 2013, 135, 18831-18839
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 18831-18839
    • Payne, C.M.1    Jiang, W.2    Shirts, M.R.3    Himmel, M.E.4    Crowley, M.F.5    Beckham, G.T.6
  • 86
    • 73649106924 scopus 로고    scopus 로고
    • High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose
    • Igarashi, K.; Koivula, A.; Wada, M.; Kimura, S.; Penttilä, M.; Samejima, M. High Speed Atomic Force Microscopy Visualizes Processive Movement of Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose J. Biol. Chem. 2009, 284, 36186-36190
    • (2009) J. Biol. Chem. , vol.284 , pp. 36186-36190
    • Igarashi, K.1    Koivula, A.2    Wada, M.3    Kimura, S.4    Penttilä, M.5    Samejima, M.6
  • 87
    • 84874159970 scopus 로고    scopus 로고
    • Initial Recognition of a Cellodextrin Chain in the Cellulose-Binding Tunnel May Affect Cellobiohydrolase Directional Specificity
    • Ghattyvenkatakrishna, P. K.; Alekozai, E. M.; Beckham, G. T.; Schulz, R.; Crowley, M. F.; Uberbacher, E. C.; Cheng, X. Initial Recognition of a Cellodextrin Chain in the Cellulose-Binding Tunnel May Affect Cellobiohydrolase Directional Specificity Biophys. J. 2013, 104, 904-912
    • (2013) Biophys. J. , vol.104 , pp. 904-912
    • Ghattyvenkatakrishna, P.K.1    Alekozai, E.M.2    Beckham, G.T.3    Schulz, R.4    Crowley, M.F.5    Uberbacher, E.C.6    Cheng, X.7
  • 88
    • 84902689475 scopus 로고    scopus 로고
    • Carbohydrate-Protein Interactions That Drive Processive Polysaccharide Translocation in Enzymes Revealed From a Computational Study of Cellobiohydrolase Processivity
    • Knott, B. C.; Crowley, M. F.; Himmel, M. E.; Stahlberg, J.; Beckham, G. T. Carbohydrate-Protein Interactions That Drive Processive Polysaccharide Translocation in Enzymes Revealed From a Computational Study of Cellobiohydrolase Processivity J. Am. Chem. Soc. 2014, 136, 8810-8819
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8810-8819
    • Knott, B.C.1    Crowley, M.F.2    Himmel, M.E.3    Stahlberg, J.4    Beckham, G.T.5
  • 91
    • 85027931281 scopus 로고    scopus 로고
    • The Role of Product Inhibition as a Yield-Determining Factor in Enzymatic High-Solid Hydrolysis of Pretreated Corn Stover
    • Olsen, S. N.; Borch, K.; Cruys-Bagger, N.; Westh, P. The Role of Product Inhibition as a Yield-Determining Factor in Enzymatic High-Solid Hydrolysis of Pretreated Corn Stover Appl. Biochem. Biotechnol. 2014, 174, 146-155
    • (2014) Appl. Biochem. Biotechnol. , vol.174 , pp. 146-155
    • Olsen, S.N.1    Borch, K.2    Cruys-Bagger, N.3    Westh, P.4
  • 92
    • 0000091593 scopus 로고
    • Nojirimycin and D-Glucono-1,5-Lactone as Inhibitors of Carbohydrases
    • Reese, E.; Parrish, F.; Ettlinger, M. Nojirimycin and D-Glucono-1,5-Lactone as Inhibitors of Carbohydrases Carbohydr. Res. 1971, 18, 381-388
    • (1971) Carbohydr. Res. , vol.18 , pp. 381-388
    • Reese, E.1    Parrish, F.2    Ettlinger, M.3
  • 93
    • 0032053577 scopus 로고    scopus 로고
    • Cellobiose Dehydrogenase Enhances Phanerochaete chrysosporium Cellobiohydrolase I Activity by Relieving Product Inhibition
    • Igarashi, K.; Samejima, M.; Eriksson, K. E. Cellobiose Dehydrogenase Enhances Phanerochaete chrysosporium Cellobiohydrolase I Activity by Relieving Product Inhibition Eur. J. Biochem. 1998, 253, 101-106
    • (1998) Eur. J. Biochem. , vol.253 , pp. 101-106
    • Igarashi, K.1    Samejima, M.2    Eriksson, K.E.3
  • 94
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen Bonding Stabilizes Globular Proteins
    • Myers, J. K.; Pace, C. N. Hydrogen Bonding Stabilizes Globular Proteins Biophys. J. 1996, 71, 2033-2039
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 96
    • 0022004957 scopus 로고
    • Detection and Differentiation of Cellulase Components Using Low Molecular Mass Fluorogenic Substrates
    • van Tilbeurgh, H.; Claeyssens, M. Detection and Differentiation of Cellulase Components Using Low Molecular Mass Fluorogenic Substrates FEBS Lett. 1985, 187, 283-288
    • (1985) FEBS Lett. , vol.187 , pp. 283-288
    • Van Tilbeurgh, H.1    Claeyssens, M.2
  • 97
    • 0021954189 scopus 로고
    • Studies of the Cellulolytic System of Trichoderma reesei QM 9414. Reaction Specificity and Thermodynamics of Interactions of Small Substrates and Ligands With the 1,4-β-glucan Cellobiohydrolase II
    • van Tilbeurgh, H.; Pettersson, G.; Bhikabhai, R.; De Boeck, H.; Claeyssens, M. Studies of the Cellulolytic System of Trichoderma reesei QM 9414. Reaction Specificity and Thermodynamics of Interactions of Small Substrates and Ligands With the 1,4-β-glucan Cellobiohydrolase II Eur. J. Biochem. 1985, 148, 329-334
    • (1985) Eur. J. Biochem. , vol.148 , pp. 329-334
    • Van Tilbeurgh, H.1    Pettersson, G.2    Bhikabhai, R.3    De Boeck, H.4    Claeyssens, M.5
  • 98
    • 79955971297 scopus 로고    scopus 로고
    • Probing Carbohydrate Product Expulsion From a Processive Cellulase With Multiple Absolute Binding Free Energy Methods
    • Bu, L.; Beckham, G. T.; Shirts, M. R.; Nimlos, M. R.; Adney, W. S.; Himmel, M. E.; Crowley, M. F. Probing Carbohydrate Product Expulsion From a Processive Cellulase With Multiple Absolute Binding Free Energy Methods J. Biol. Chem. 2011, 286, 18161-18169
    • (2011) J. Biol. Chem. , vol.286 , pp. 18161-18169
    • Bu, L.1    Beckham, G.T.2    Shirts, M.R.3    Nimlos, M.R.4    Adney, W.S.5    Himmel, M.E.6    Crowley, M.F.7
  • 100
    • 78650950110 scopus 로고    scopus 로고
    • Processivity of Cellobiohydrolases Is Limited by the Substrate
    • Kurašin, M.; Väljamäe, P. Processivity of Cellobiohydrolases Is Limited by the Substrate J. Biol. Chem. 2011, 286, 169-177
    • (2011) J. Biol. Chem. , vol.286 , pp. 169-177
    • Kurašin, M.1    Väljamäe, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.