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Results: 1-25 | 26-31
Results: 1-25/31
Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin
Authors: Craig, DH Barna, T Moody, PCE Bruce, NC Chapman, SK Munro, AW Scrutton, NS
Citation: Dh. Craig et al., Effects of environment on flavin reactivity in morphinone reductase: analysis of enzymes displaying differential charge near the N-1 atom and C-2 carbonyl region of the active-site flavin, BIOCHEM J, 359, 2001, pp. 315-323
Kinetics of CO binding to the haem domain of murine inducible nitric oxidesynthase: differential effects of haem domain ligands
Authors: Stevenson, TH Gutierrez, AF Alderton, WK Lian, LY Scrutton, NS
Citation: Th. Stevenson et al., Kinetics of CO binding to the haem domain of murine inducible nitric oxidesynthase: differential effects of haem domain ligands, BIOCHEM J, 358, 2001, pp. 201-208
Kinetics of CO binding and CO photodissociation in Pseudomonas stutzeri cd(1) nitrile reductase: probing the role of extended N-termini in fast structural relaxation upon CO photodissociation (vol 355, pg 39, 2001)
Authors: Wilson, EK Bellelli, A Cutruzzola, F Zumft, WG Gutierrez, A Scrutton, NS
Citation: Ek. Wilson et al., Kinetics of CO binding and CO photodissociation in Pseudomonas stutzeri cd(1) nitrile reductase: probing the role of extended N-termini in fast structural relaxation upon CO photodissociation (vol 355, pg 39, 2001), BIOCHEM J, 356, 2001, pp. 911-911
Kinetics of CO binding and CO photodissociation in Pseudomonas stutzeri cd(1) nitrite reductase: probing the role of extended N-termini in fast structural relaxation upon CO photodissociation
Authors: Wilson, EK Bellelli, A Cutruzzola, F Zumft, WG Gutierrez, A Scrutton, NS
Citation: Ek. Wilson et al., Kinetics of CO binding and CO photodissociation in Pseudomonas stutzeri cd(1) nitrite reductase: probing the role of extended N-termini in fast structural relaxation upon CO photodissociation, BIOCHEM J, 355, 2001, pp. 39-43
Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characterization of the individual iron-binding domains by optical, CD and NMR spectroscopies
Authors: Perry, A Lian, LY Scrutton, NS
Citation: A. Perry et al., Two-iron rubredoxin of Pseudomonas oleovorans: production, stability and characterization of the individual iron-binding domains by optical, CD and NMR spectroscopies, BIOCHEM J, 354, 2001, pp. 89-98
Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme
Authors: Barna, TM Khan, H Bruce, NC Barsukov, I Scrutton, NS Moody, PCE
Citation: Tm. Barna et al., Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme, J MOL BIOL, 310(2), 2001, pp. 433-447
Importance of barrier shape in enzyme-catalyzed reactions - Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent aminedehydrogenases
Authors: Basran, J Patel, S Sutcliffe, MJ Scrutton, NS
Citation: J. Basran et al., Importance of barrier shape in enzyme-catalyzed reactions - Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent aminedehydrogenases, J BIOL CHEM, 276(9), 2001, pp. 6234-6242
Optimizing the Michaelis complex of trimethylamine dehydrogenase - Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base
Authors: Basran, J Sutcliffe, MJ Scrutton, NS
Citation: J. Basran et al., Optimizing the Michaelis complex of trimethylamine dehydrogenase - Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base, J BIOL CHEM, 276(46), 2001, pp. 42887-42892
Protein dynamics enhance electronic coupling in electron transfer complexes
Authors: Chohan, KK Jones, M Grossmann, JG Frerman, FE Scrutton, NS Sutcliffe, MJ
Citation: Kk. Chohan et al., Protein dynamics enhance electronic coupling in electron transfer complexes, J BIOL CHEM, 276(36), 2001, pp. 34142-34147
Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase - Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes
Authors: Basran, J Sutcliffe, MJ Scrutton, NS
Citation: J. Basran et al., Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase - Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes, J BIOL CHEM, 276(27), 2001, pp. 24581-24587
alpha Arg-237 in Methylophilus methylotrophus (sp W3A1) electron-transferring flavoprotein affords similar to 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone
Authors: Talfournier, F Munro, AW Basran, J Sutcliffe, MJ Daff, S Chapman, SK Scrutton, NS
Citation: F. Talfournier et al., alpha Arg-237 in Methylophilus methylotrophus (sp W3A1) electron-transferring flavoprotein affords similar to 200-millivolt stabilization of the FAD anionic semiquinone and a kinetic block on full reduction to the dihydroquinone, J BIOL CHEM, 276(23), 2001, pp. 20190-20196
Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp. - Implications for glycine betaine catabolism
Authors: Meskys, R Harris, RJ Casaite, V Basran, J Scrutton, NS
Citation: R. Meskys et al., Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp. - Implications for glycine betaine catabolism, EUR J BIOCH, 268(12), 2001, pp. 3390-3398
Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains
Authors: Gutierrez, A Lian, LY Wolf, CR Scrutton, NS Roberts, GCK
Citation: A. Gutierrez et al., Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains, BIOCHEM, 40(7), 2001, pp. 1964-1975
QM/MM studies show substantial tunneling for the hydrogen-transfer reaction in methylamine dehydrogenase
Authors: Faulder, PF Tresadern, G Chohan, KK Scrutton, NS Sutcliffe, MJ Hillier, IH Burton, NA
Citation: Pf. Faulder et al., QM/MM studies show substantial tunneling for the hydrogen-transfer reaction in methylamine dehydrogenase, J AM CHEM S, 123(35), 2001, pp. 8604-8605
Enzyme catalysis: over-the-barrier or through-the-barrier?
Authors: Sutcliffe, MJ Scrutton, NS
Citation: Mj. Sutcliffe et Ns. Scrutton, Enzyme catalysis: over-the-barrier or through-the-barrier?, TRENDS BIOC, 25(9), 2000, pp. 405-408
X-ray scattering studies of Methylophilus methylotrophus (sp W(3)A(1)) electron-transferring flavoprotein - Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase
Authors: Jones, M Basran, J Sutcliffe, MJ Grossmann, JG Scrutton, NS
Citation: M. Jones et al., X-ray scattering studies of Methylophilus methylotrophus (sp W(3)A(1)) electron-transferring flavoprotein - Evidence for multiple conformational states and an induced fit mechanism for assembly with trimethylamine dehydrogenase, J BIOL CHEM, 275(28), 2000, pp. 21349-21354
Formation of W(3)A(1) electron-transferring flavoprotein (ETF) hydroquinone in the trimethylamine dehydrogenase center dot ETF protein complex
Authors: Jang, MH Scrutton, NS Hille, R
Citation: Mh. Jang et al., Formation of W(3)A(1) electron-transferring flavoprotein (ETF) hydroquinone in the trimethylamine dehydrogenase center dot ETF protein complex, J BIOL CHEM, 275(17), 2000, pp. 12546-12552
Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp 1-IN
Authors: Harris, RJ Meskys, R Sutcliffe, MJ Scrutton, NS
Citation: Rj. Harris et al., Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp 1-IN, BIOCHEM, 39(6), 2000, pp. 1189-1198
Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: Properties of the soluble W676Rand W676A mutant reductases
Authors: Gutierrez, A Doehr, O Paine, M Wolf, CR Scrutton, NS Roberts, GCK
Citation: A. Gutierrez et al., Trp-676 facilitates nicotinamide coenzyme exchange in the reductive half-reaction of human cytochrome P450 reductase: Properties of the soluble W676Rand W676A mutant reductases, BIOCHEM, 39(51), 2000, pp. 15990-15999
Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein
Authors: Basran, J Chohan, KK Sutcliffe, MJ Scrutton, NS
Citation: J. Basran et al., Differential coupling through Val-344 and Tyr-442 of trimethylamine dehydrogenase in electron transfer reactions with ferricenium ions and electron transferring flavoprotein, BIOCHEM, 39(31), 2000, pp. 9188-9200
Redox cycles in trimethylamine dehydrogenase and mechanism of substrate inhibition (vol 38, pg 14927, 1999)
Authors: Roberts, P Basran, J Wilson, EK Hille, R Scrutton, NS
Citation: P. Roberts et al., Redox cycles in trimethylamine dehydrogenase and mechanism of substrate inhibition (vol 38, pg 14927, 1999), BIOCHEM, 39(3), 2000, pp. 625-625
Structural and biochemical characterization of recombinant wild type and aC30A mutant of trimethylamine dehydrogenase from Methylphilus methylotrophus (sp W(3)A(1))
Authors: Trickey, P Basran, J Lian, LY Chen, ZW Barton, JD Sutcliffe, MJ Scrutton, NS Mathews, FS
Citation: P. Trickey et al., Structural and biochemical characterization of recombinant wild type and aC30A mutant of trimethylamine dehydrogenase from Methylphilus methylotrophus (sp W(3)A(1)), BIOCHEM, 39(26), 2000, pp. 7678-7688
Enzymes in the quantum world
Authors: Scrutton, NS
Citation: Ns. Scrutton, Enzymes in the quantum world, BIOCH SOC T, 27, 1999, pp. 767-779
Electron transfer in trimethylamine dehydrogenase and electron-transferring flavoprotein
Authors: Scrutton, NS Basran, J Wilson, EK Chohan, KK Jang, MH Sutcliffe, MJ Hille, R
Citation: Ns. Scrutton et al., Electron transfer in trimethylamine dehydrogenase and electron-transferring flavoprotein, BIOCH SOC T, 27(2), 1999, pp. 196-201
Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex
Authors: Basran, J Sutcliffe, MJ Hille, R Scrutton, NS
Citation: J. Basran et al., Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex, BIOCHEM J, 341, 1999, pp. 307-314
Risultati: 1-25 | 26-31