Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.

@article{Enguita2004SubstrateAD,
  title={Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.},
  author={Francisco Javier Enguita and David Marçal and L{\'i}gia O. Martins and Rosa Grenha and Adriano O Henriques and Peter F. Lindley and Maria Arm{\'e}nia Carrondo},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 22},
  pages={23472-6}
}
The CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the non-catalytic co-oxidant 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS), and the structure was determined using synchrotron radiation. The binding site for this adduct is well defined and indicates how ABTS, in conjunction with laccases, could act as an oxidative mediator toward non-phenolic moieties. In addition, a dioxygen moiety is clearly defined within the solvent channel… CONTINUE READING

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