A strong H-bond between a cysteine and the catalytic center of a [NiFe]-hydrogenase
Infrared spectroscopy at cryogenic temperatures was used to monitor protonation changes on an H<sup>+</sup>-accepting, nickel-coordinating active site cysteine of the H<sub>2</sub>/H<sup>+</sup>-cycling membrane-bound [NiFe]-hydrogenase from <i>Cupriavidus necator</i>. Surprisingly, we identified another cysteine in the outer coordination sphere forming a strong H-bond with a cysteine thiolate coordinating both nickel and iron of the catalytic center.
Authors
- Chara Karafoulidi‐Retsou (ORCID: https://orcid.org/0000-0001-8572-4080)
- Oliver Lenz (ORCID: https://orcid.org/0000-0003-4550-5128)
- Stefan Frielingsdorf (ORCID: https://orcid.org/0000-0002-4141-7836)
- Giorgio Caserta (ORCID: https://orcid.org/0000-0003-0986-3059)
- Ingo Zebger (ORCID: https://orcid.org/0000-0002-6354-3585)
- Sagie Katz (ORCID: https://orcid.org/0000-0001-8526-183X)
Institutions
- Technische Universität Berlin (DE)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5cc00646e
- Citations
- 3
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 1.09