Laccase Redox Potentials: pH Dependence and Mutants, a QM/MM Study.

@article{Gtze2016LaccaseRP,
  title={Laccase Redox Potentials: pH Dependence and Mutants, a QM/MM Study.},
  author={Jan P. G{\"o}tze and Michael B{\"u}hl},
  journal={The journal of physical chemistry. B},
  year={2016},
  volume={120 35},
  pages={
          9265-76
        }
}
We have studied the T. versicolor laccase T1 site redox potential (RP) at the M06/6-311++G**/SDD(Cu) level of theory, employing QM/MM-optimized geometries (RI-BP86/def2-SVP/def2-TZVP(Cu):CHARMM) of the whole protein system with electronic embedding. The oxidation state of the trinuclear cluster was found to affect the T1 site RP by about 0.2-0.3 V, depending on the protein protonation state. The computed laccase RP can be drastically lowered upon introduction of a protonation state… CONTINUE READING

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