封面专题：了解钒氮酶的 P 簇：酶的 Holo 与 Apo 形态的 EPR 和 XAS 研究（ChemBioChem 3/2025）

IF 2.6 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

ChemBioChem Pub Date : 2025-02-13 DOI:10.1002/cbic.202580302

Isis M. Wahl, Kushal Sengupta, Maurice van Gastel, Laure Decamps, Serena DeBeer

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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)

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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.

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来源期刊

ChemBioChem 生物-生化与分子生物学

CiteScore

6.10

自引率

3.10%

发文量

407

审稿时长

1 months

期刊介绍： 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).