Model compound met the key structural and spectroscopic features of [FeFe]-hydrogenase active site

2019 · doi:10.3762/bxiv.2019.136.v1
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A synthesized iron complex, Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM), replicates the structural and spectroscopic features of the [FeFe]-hydrogenase active site and exhibits low oxidation potentials.

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The paper studies a biomimetic model compound, Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM), designed to replicate key structural features of the natural [FeFe]-hydrogenase active site. Using spectroscopic comparisons, it reports that the IR wavenumbers of the model compound closely match those of the natural active site, and it measures low oxidation potentials at −0.48 V and −0.26 V. The authors attribute improved stability of an “open site” in a rotated structure to ethyl assistance in the S–S bridging framework and to sterically encumbering, electron-rich ligand substitutions. A major caveat is that the work is presented as an unreviewed preprint. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

Biomimetic synthesis of the [FeFe]-hydrogenase active site draws considerable attention of scientists for its amazing catalytic efficiency on reversible transition between proton and hydrogen. Fe 2 (CO) 3 [μ-(SCH(CH 2 CH 3 )CH 2 S)](μ-DPPM)(κ 1 -DPPM) (compound 1 ) which replicated key structural aspects of the natural [FeFe]-hydrogenase was designed and synthesized. 1 showed that the wavenumbers in IR were close to those of the natural [FeFe]-hydrogenase active site. In addition, 1 achieved the low oxidation potentials at -0.48 V and -0.26 V, respectively. In the assistance of ethyl located in the S-S bridging structure, the asymmetrical substitution with sterically encumbering and electron-rich ligands in 1 may offer a thorough protection for forming and stabilizing the open site in the rotated structure.
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Materials

chemistry Medicinal and pharmaceutical chemistry Nano- and molecular-scale electronics Nano-biomaterials and bioscience Nanomagnetics Nanomaterials, thin films and nanointerfaces Nanomedicine Nanometrology and nanomechanics Nano-optics Nanopatterning, self-assembly and nanofabrication Nanostructures for energy and sensing applications Natural products chemistry Organo main group chemistry Other nanotechnology (unclassified) Other organic chemistry (unclassified) Photochemistry and photovoltaics Physical organic chemistry Supramolecular chemistry Biomimetic synthesis of the [FeFe]-hydrogenase active site draws considerable attention of scientists for its amazing catalytic efficiency on reversible transition between proton and hydrogen. Fe2(CO)3[μ-(SCH(CH2CH3)CH2S)](μ-DPPM)(κ1-DPPM) (compound 1) which replicated key structural aspects of the natural [FeFe]-hydrogenase was designed and synthesized. 1 showed that the wavenumbers in IR were close to those of the natural [FeFe]-hydrogenase active site. In addition, 1 achieved the low oxidation potentials at -0.48 V and -0.26 V, respectively. In the assistance of ethyl located in the S-S bridging structure, the asymmetrical substitution with sterically encumbering and electron-rich ligands in 1 may offer a thorough protection for forming and stabilizing the open site in the rotated structure.

Keywords

[FeFe]-hydrogenase; Structure simulation; Model compound; Enzymes; Oxidation potential | Format: DOCX | Size: 799.2 KB | Download | When a peer-reviewed version of this preprint is available, this information will be updated in the information box above. If no peer-reviewed version is available, please cite this preprint using the following information: Hai, L.; Zhang, T.; Jiang, S.; Ma, X.; Wang, D.; Li, B. Beilstein Arch. 2019, 2019136. doi:10.3762/bxiv.2019.136.v1 Citation data can be downloaded as file using the "Download" button or used for copy/paste from the text window below. Citation data in RIS format can be imported by all major citation management software, including EndNote, ProCite, RefWorks, and Zotero. © 2019 Hai et al.; licensee Beilstein-Institut. This is an Open Access article under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0). Please note that the reuse, redistribution and reproduction in particular requires that the authors and source are credited. The license is subject to the Beilstein Archives terms and conditions: (https://www.beilstein-archives.org/xiv/terms)

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