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Issue 32, 2019
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Insights from 125Te and 57Fe nuclear resonance vibrational spectroscopy: a [4Fe–4Te] cluster from two points of view

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Abstract

Iron–sulfur clusters are common building blocks for electron transport and active sites of metalloproteins. Their comprehensive investigation is crucial for understanding these enzymes, which play important roles in modern biomimetic catalysis and biotechnology applications. We address this issue by utilizing (Et4N)3[Fe4Te4(SPh)4], a tellurium modified version of a conventional reduced [4Fe–4S]+ cluster, and performed both 57Fe- and 125Te-NRVS to reveal its characteristic vibrational features. Our analysis exposed major differences in the resulting 57Fe spectrum profile as compared to that of the respective [4Fe–4S] cluster, and between the 57Fe and 125Te profiles. DFT calculations are applied to rationalize structural, electronic, vibrational, and redox-dependent properties of the [4Fe–4Te]+ core. We herein highlight the potential of sulfur/tellurium exchange as a method to isolate the iron-only motion in enzymatic systems.

Graphical abstract: Insights from 125Te and 57Fe nuclear resonance vibrational spectroscopy: a [4Fe–4Te] cluster from two points of view

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Article information


Submitted
24 Apr 2019
Accepted
22 Jun 2019
First published
24 Jun 2019

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2019,10, 7535-7541
Article type
Edge Article

Insights from 125Te and 57Fe nuclear resonance vibrational spectroscopy: a [4Fe–4Te] cluster from two points of view

F. Wittkamp, N. Mishra, H. Wang, H. Wille, R. Steinbrügge, M. Kaupp, S. P. Cramer, U. Apfel and V. Pelmenschikov, Chem. Sci., 2019, 10, 7535
DOI: 10.1039/C9SC02025J

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