Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis

Ferran Planas, Michael J McLeish, Fahmi Himo

Open source

DOI
10.3762/bjoc.15.15
Published
2019-01-16
Container
Beilstein Journal of Organic Chemistry
Publisher
Beilstein Institut
Open access
unknown

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BibTeX

@article{allodium:10.3762/bjoc.15.15,
  title = {Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis},
  author = {Ferran Planas and Michael J McLeish and Fahmi Himo},
  year = {2019},
  journal = {Beilstein Journal of Organic Chemistry},
  doi = {10.3762/bjoc.15.15},
  url = {https://doi.org/10.3762/bjoc.15.15}
}

RIS

TY  - JOUR
TI  - Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis
AU  - Ferran Planas
AU  - Michael J McLeish
AU  - Fahmi Himo
PY  - 2019
JO  - Beilstein Journal of Organic Chemistry
DO  - 10.3762/bjoc.15.15
UR  - https://doi.org/10.3762/bjoc.15.15
ER  - 

APA

Planas, F., McLeish, M. J., & Himo, F. (2019). Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis. Beilstein Journal of Organic Chemistry. https://doi.org/10.3762/bjoc.15.15

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