Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2015 ]
Poraj-Kobielska M, Peter S, Leonhardt S, Ullrich R, Scheibner K, Hofrichter M Immobilization of unspecific peroxygenases (EC 1.11.2.1) in PVA/PEG gel and hollow fiber modules
Biochem. Eng. J., 98: 144-150
[ 2015 ]
Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A In-Depth 2D NMR Study of Lignin Modification During Pretreatment of Eucalyptus Wood with Laccase and Mediators
Bioenerg. Res., 8: 211-230
[ 2015 ]
Saez-Jimenez V, Acebes S, Guallar V, Martínez AT, Ruiz-Dueñas FJ Improving the oxidative stability of a high redox potential fungal peroxidase by rational design
PlosOne, 10-4
[ 2015 ]
Saez-Jimenez V, Baratto MC, Pogni R, Rencoret J, Gutiérrez A, Santos JI, Martínez AT, Ruiz-Dueñas FJ Demonstration of Lignin-to-Peroxidase Direct Electron Transfer: A Transient-state Kinetics, Directed Mutagenesis, EPR and NMR Study
J. Biol. Chem., 290: 23201-23213
[ 2015 ]
Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ, Romero A, Martínez AT, Ruiz-Dueñas FJ Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase
PlosOne, doi: 10.1371/journal.pone.0140984
[ 2015 ]
Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hällberg BM, Ludwig R, Divine C Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation
Nat. Commun., 6: 7542
year2015
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive
Wang X, Ullrich R, Hofrichter M, Groves JT
Proc. Natl. Acad. Sci. USA, 112: 3686-3691
The heme-thiolate peroxygenase of Agrocybe aegerita is a remarkably capable biocatalyst and a mechanistic analog of cytochrome P450. The stability of this fungal protein has provided a rare opportunity to study P450-like C−H hydroxylation in a novel and unrelated enzyme. Both APO-I and APO-II have been generated, and their redox potentials have been determined. The ferryl species Cys−S−FeIV−OH (APO-II) has been generated cleanly via reduction of the corresponding APO-I and a basic pKa revealed for the Cys−S−FeIV−OH ⇄ Cys−S−FeIV=O equilibrium. Most significantly, APO-II displays surprisingly high reactivity toward benzylic C−H (bond-dissociation energy 80−86 kcal/mol) and phenolic substrates with rate constants orders of magnitude larger than those of typical peroxidases or model compounds due to the basic ferryl.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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