| Title: |
Distinct Valence States of the [4Fe4S] Cluster Revealed in the Hydrogenase CrHydA1. |
| Authors: |
Heghmanns, Melanie1 (AUTHOR), Yadav, Shalini2 (AUTHOR), Boschmann, Sergius1 (AUTHOR), Selve, Victor R.1 (AUTHOR), Veliju, Astrit3 (AUTHOR), Brocks, Claudia3 (AUTHOR), Happe, Thomas3 (AUTHOR), Pantazis, Dimitrios A.2 (AUTHOR) dimitrios.pantazis@kofo.mpg.de, Kasanmascheff, Müge1 (AUTHOR) muege.kasanmascheff@tu-dortmund.de |
| Source: |
Angewandte Chemie International Edition. Jan2025, p1. 12p. 7 Illustrations, 1 Chart. |
| Abstract: |
Iron‐sulfur clusters play a crucial role in electron transfer for many essential enzymes, including [FeFe]‐hydrogenases. This study focuses on the [4Fe4S] cluster ([4Fe]H) of the minimal [FeFe]‐hydrogenase from Chlamydomonas reinhardtii (CrHydA1) and employs advanced spectroscopy, site‐directed mutagenesis, molecular dynamics simulations, and QM/MM calculations. We provide insights into the complex electronic structure of [4Fe]H and its role in the catalytic reaction of CrHydA1, serving as paradigm for understanding [FeFe]‐hydrogenases. We identified at least two distinct species within the apo‐form of CrHydA1, designated 4Fe−R and 4Fe−A, with unique redox potentials and pH sensitivities. Our findings revealed that these species arise from a complex interplay of structural heterogeneity and valence isomer rearrangements, influenced by second‐sphere residues. We propose that the interconversion between 4Fe−R and 4Fe−A could provide control over electron transfer in the absence of accessory FeS clusters typically found in other [FeFe]‐hydrogenases. The insights gained from this study not only enhance our understanding of [FeFe]‐hydrogenases but also provide a crucial foundation for future investigations into analysis of other FeS clusters across diverse biological systems. [ABSTRACT FROM AUTHOR] |
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