| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5381836 | Chemical Physics Letters | 2013 | 4 Pages |
Abstract
- The active site of [NiFe]-hydrogenase is studied with electronic structure methods.
- Rotation of thiolate ligands makes either singlet or triplet state a ground state.
- At the experimental ligand orientation the two states become quasidegenerate.
- We discuss the implication of this degeneracy for nonadiabatic hydrogen catalysis.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
![Protein induced singlet-triplet quasidegeneracy in the active site of [NiFe]-hydrogenase](/preview/png/5381836.png "First Page Preview: Protein induced singlet-triplet quasidegeneracy in the active site of [NiFe]-hydrogenase")
Authors
Renante L. Yson, Jessica L. Gilgor, Benjamin A. Guberman, Sergey A. Varganov,