Cover Feature: Understanding the P‐Cluster of Vanadium Nitrogenase: an EPR and XAS Study of the Holo vs. Apo Forms of the Enzyme (ChemBioChem 3/2025)
The cover illustrates the structure of the P-cluster, one of the two Fe-S clusters present in the catalytic moiety of nitrogenase. The background illustration is the vanadium nitrogenase catalytic component (VFe), which is the focus of article 10.1002/cbic.202400833. In this work, Laure Decamps, Serena DeBeer, and co-workers combine biochemical, electron paramagnetic resonance (EPR) spectroscopy, and extended X-ray absorption fine structure (EXAFS) data to shed light on open questions about the structural differences between the holo and apo forms of VFe.
Authors
- Maurice van Gastel (ORCID: https://orcid.org/0000-0002-1547-6365)
- Kushal Sengupta (ORCID: https://orcid.org/0000-0002-5941-406X)
- Serena DeBeer (ORCID: https://orcid.org/0000-0002-5196-3400)
- Laure Decamps (ORCID: https://orcid.org/0000-0002-4572-7479)
- Isis Mani Wahl (ORCID: https://orcid.org/0000-0001-5074-7493)
Institutions
- Max-Planck-Institut für Kohlenforschung (DE)
- Max Planck Institute for Chemical Energy Conversion (DE)
Publication Details
- Journal
- ChemBioChem
- Published
- 2025-02-01
- DOI
- https://doi.org/10.1002/cbic.202580302
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00