0 Datasets
0 Files
Get instant academic access to this publication’s datasets.
Yes. After verification, you can browse and download datasets at no cost. Some premium assets may require author approval.
Files are stored on encrypted storage. Access is restricted to verified users and all downloads are logged.
Yes, message the author after sign-up to request supplementary files or replication code.
Join 50,000+ researchers worldwide. Get instant access to peer-reviewed datasets, advanced analytics, and global collaboration tools.
✓ Immediate verification • ✓ Free institutional access • ✓ Global collaborationJoin our academic network to download verified datasets and collaborate with researchers worldwide.
Get Free AccessDeveloping biomimetic complexes that model the active site of [NiFe] hydrogenase enzymes in order to catalyze the activation of H2 is a topic of major interest. A functional [NiFe] hydrogenase model complex has recently been described by Ogo et al. (Science, 2013, 339, 682-683). Here, we report a Mössbauer and computational investigation of this model complex. This study affords deeper understanding of the electronic structure, the reactivity and the mechanism of H2 activation by this complex.
Amélie Kochem, Eckhard Bill, Frank Neese, Maurice van Gastel (2014). Mössbauer and computational investigation of a functional [NiFe] hydrogenase model complex. Chemical Communications, 51(11), pp. 2099-2102, DOI: 10.1039/c4cc09035g.
Datasets shared by verified academics with rich metadata and previews.
Authors choose access levels; downloads are logged for transparency.
Students and faculty get instant access after verification.
Type
Article
Year
2014
Authors
4
Datasets
0
Total Files
0
Language
English
Journal
Chemical Communications
DOI
10.1039/c4cc09035g
Access datasets from 50,000+ researchers worldwide with institutional verification.
Get Free Access
