2025/04/27 by Hongxin Wang, Vladimir Pelmenschikov, Yoshitaka Yoda +1 · 1 voice · 1 citation
Energy · Chemical Engineering · Chemistry · #Metalloenzymes and iron-sulfur proteins #Ammonia Synthesis and Nitrogen Reduction #Metal-Catalyzed Oxygenation Mechanisms
paper · doi:10.1016/j.jinorgbio.2025.112935
openalex created_date 2025/04/27 · openalex publication_date 2025/04/27 · openalex updated_date 2026/07/15
Iron‑sulfur clusters are the primordial prosthetic groups for living systems, and they have even been proposed as partly responsible for the origin of life. They play a role in essential biological processes such as electron transfer, enzyme catalysis, DNA replication and repair, small molecule sensing, iron homeostasis, apoptosis, and human health and disease. They have frequently been studied by resonance Raman, electron paramagnetic resonance, and Mössbauer spectroscopies. Over the past two decades, we have used a synchrotron method called Nuclear Resonance Vibrational Spectroscopy (NRVS) to examine the vibrational dynamics of a wide variety of FeS clusters in model systems and native proteins, ranging in complexity from single Fe sites in small rubredoxins to the [7Fe-9S-C-Mo-R-homocitrate] cluster in nitrogenases.