Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis
- 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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Cite this work
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
Source records
- crossref · retrieved 2026-09-25T19:42:59.033Z