Isis M. Wahl, Kushal Sengupta, Maurice van Gastel, Laure Decamps, Serena DeBeer
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Abstract
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.
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ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
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