Quick Review of Chemistry Related to the [Fe]-Hydrogenases
Nasser Thallaj
Prof. Dr. Nasser Thallaj, Professor, Pharmaceutical Chemistry and Drug Quality Control Department, Faculty of Pharmacy, Al-Rachid Privet University, Damascus, Syria.
Manuscript received on 03 May 2022 | Revised Manuscript received on 10 June 2022 | Manuscript Accepted on 15 June 2022 | Manuscript published on 30 June 2022 | PP: 1-15 | Volume-2 Issue-4, June 2022 | Retrieval Number: 100.1/ijapsr.C4016043323 | DOI: 10.54105/ijapsr.C4016.062422
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© The Authors. Published by Lattice Science Publication (LSP). This is an open access article under the CC-BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)
Abstract: This review provides a comprehensive overview of the synthesis, reactivity, and electrochemistry of chemical models of active site structures in [Fe] hydrogenase, an enzyme that catalyzes the reversible reduction of protons to submergence. Related literature on the structure and functions of the [Fe] hydrogenase active site, H cluster, is discussed with an emphasis on the di-iron organosome. In addition, various methods for the preparation and characterization of model complexes are discussed, as well as reactivity studies focusing on the oxidation and reduction of model compounds and their interaction with small molecules such as hydrogen and carbon monoxide. Finally, the electrochemical behavior of the model compounds is discussed in relation to their performance in electrocatalytic applications. This review provides a comprehensive analysis of the chemistry and reactivity of chemical models of the active site of [Fe] hydrogenase, which can be a valuable reference for further research.
Keywords: Fe-hydrogenase, H-cluster, Fe4S4 Cubane, Cysteinyl Bridge, Di-Iron Organometallic Subsite, Dithiolate, Iron-Sulfur Proteins.
Scope of the Article: Pharmaceutical Analysis