Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
J Am Chem Soc ; 133(13): 4802-9, 2011 Apr 06.
Article in English | MEDLINE | ID: mdl-21388209

ABSTRACT

The redox potentials and reorganization energies of the type 1 (T1) Cu site in four multicopper oxidases were calculated by combining first principles density functional theory (QM) and QM/MM molecular dynamics (MD) simulations. The model enzymes selected included the laccase from Trametes versicolor, the laccase-like enzyme isolated from Bacillus subtilis, CueO required for copper homeostasis in Escherichia coli, and the small laccase (SLAC) from Streptomyces coelicolor. The results demonstrated good agreement with experimental data and provided insight into the parameters that influence the T1 redox potential. Effects of the immediate T1 Cu site environment, including the His(N(δ))-Cys(S)-His(N(δ)) and the axial coordinating amino acid, as well as the proximate H(N)(backbone)-S(Cys) hydrogen bond, were discerned. Furthermore, effects of the protein backbone and side-chains, as well as of the aqueous solvent, were studied by QM/MM molecular dynamics (MD) simulations, providing an understanding of influences beyond the T1 Cu coordination sphere. Suggestions were made regarding an increase of the T1 redox potential in SLAC, i.e., of Met198 and Thr232 in addition to the axial amino acid Met298. Finally, the results of this work presented a framework for understanding parameters that influence the Type 1 Cu MCO redox potential, useful for an ever-growing range of laccase-based applications.


Subject(s)
Molecular Dynamics Simulation , Oxidoreductases/metabolism , Crystallography, X-Ray , Models, Molecular , Oxidation-Reduction , Oxidoreductases/chemistry , Quantum Theory
2.
Chem Commun (Camb) ; 46(33): 6045-7, 2010 Sep 07.
Article in English | MEDLINE | ID: mdl-20571702

ABSTRACT

Multicopper oxidases linked to multiwall carbon nanotubes via the molecular tethering reagent, 1-pyrenebutanoic acid, succinimidyl ester, displayed high bioelectrocatalytic activity for oxygen reduction.


Subject(s)
Enzymes, Immobilized/chemistry , Nanotubes, Carbon/chemistry , Oxidoreductases/chemistry , Bioelectric Energy Sources , Catalysis , Electrochemistry , Electrodes , Electron Transport , Oxygen/chemistry , Pyrenes/chemistry , Substrate Specificity
SELECTION OF CITATIONS
SEARCH DETAIL
...