Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
about
Nitroaromatic compounds, from synthesis to biodegradationEngineering non-heme mono- and dioxygenases for biocatalysisStructural Basis of the Divergent Oxygenation Reactions Catalyzed by the Rieske Nonheme Iron Oxygenase Carbazole 1,9a-DioxygenaseEnhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere InteractionsStructural and functional studies of ferredoxin and oxygenase components of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.Molecular Dynamics Simulation of Nitrobenzene Dioxygenase Using AMBER Force FieldSelection for growth on 3-nitrotoluene by 2-nitrotoluene-utilizing Acidovorax sp. strain JS42 identifies nitroarene dioxygenases with altered specificities.Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase.Application of nitroarene dioxygenases in the design of novel strains that degrade chloronitrobenzenes.Emerging technologies in bioremediation: constraints and opportunities.A DFT study of the cis-dihydroxylation of nitroaromatic compounds catalyzed by nitrobenzene dioxygenase.Probing the molecular determinants of aniline dioxygenase substrate specificity by saturation mutagenesis.Reconstructing the evolutionary history of nitrotoluene detection in the transcriptional regulator NtdR.Evolution of a new bacterial pathway for 4-nitrotoluene degradation.A DFT and ONIOM study of C-H hydroxylation catalyzed by nitrobenzene 1,2-dioxygenase.Directed evolution of nitrobenzene dioxygenase for the synthesis of the antioxidant hydroxytyrosol.
P2860
Q24594536-B7CCDC89-DDCF-4BD6-AFDE-CAFD0FDAF27CQ27022534-9DAEE5EB-6419-421E-9AAE-924E0347A5F2Q27681938-6C3E85DA-EFEE-4041-8688-67BDEFEFC3BBQ27704037-FD154942-BE8B-4230-9EA3-7154FB38FFDCQ33610272-DB19F470-24B5-4FE2-B5C7-BABCF4CA4309Q33761734-22ADFB32-FF13-4CA8-8E55-A84F6A660942Q34747563-835F2FC4-4E89-4F42-B26B-4FF82595B4D3Q35075667-BA9EF51B-93DB-4FCC-BBED-1A17FBBD362DQ37274781-722FEB83-41DC-433E-BD3A-4EFCDDA4EC4DQ38029951-913FCB8B-6845-47CE-8790-9120F16B3FF0Q38569964-56C703D1-EF50-4915-8CDE-44900884C7DAQ40246428-9D8D81A5-BA5A-4616-836B-5A0DF4D1205BQ43256702-A3C553CC-C7EA-45FA-B461-D455AA6F9050Q46272784-151FD15A-03F2-4869-B72C-A13921B9004AQ46884110-7EEDE16D-8846-492D-89EE-5EBA65D7A0A5Q53632644-95345F64-D541-41E9-ABE3-9F3255238E7C
P2860
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@en
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@nl
type
label
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@en
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@nl
prefLabel
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@en
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@nl
P2860
P1476
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase.
@en
P2093
Kou-San Ju
Rebecca E Parales
P2860
P304
P356
10.1128/AEM.72.3.1817-1824.2006
P407
P577
2006-03-01T00:00:00Z