Work

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)

Year: 2025

Type: article

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.

Source: ChemBioChem

DOI: 10.1002/cbic.202580302

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

Institutions: Max Planck Institute for Chemical Energy Conversion, Max-Planck-Institut für Kohlenforschung

Language: English

Topic: Metalloenzymes and iron-sulfur proteins

Subfield: Renewable Energy, Sustainability and the Environment

Field: Energy

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W4407536005

FWCI:

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