Synthetic Models for Nickel–Iron Hydrogenase Featuring Redox-Active Ligands

Schilter, David; Gray, Danielle L.; Fuller, Amy L.; Rauchfuss, Thomas B.

doi:10.1071/ch16614

Cited by 3 publications

(2 citation statements)

References 47 publications

(68 reference statements)

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“…Thus, it is adequate to obtain mechanistic insights from a biomimetic model as an initial step. To understand the complicated redox process in hydrogenases, , the experimentalists have synthesized a variety of biomimetic models including both catalytic center and cofactor which relate to the redox process in NiFe, Fe-Fe, and Fe-only hydrogenases. − Furthermore, theoretical calculations have been conducted to obtain mechanistic insight into the redox processes. , …”

Section: Introductionmentioning

confidence: 99%

Electron and Hydride Transfer in a Redox-Active NiFe Hydride Complex: A DFT Study

et al. 2018

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We present mechanistic details of the formation of a NiFe hydride complex and provide information on its electron-and hydride-transfer processes on the basis of density functional theory calculations and artificial-forceinduced-reaction studies. The NiFe hydride complex conducts three transfer reactions: namely, electron transfer, hydride transfer, and proton transfer. In a NiFe hydride complex, the hydride binds to Fe, which is different from the Ni−R state in hydrogenase where the hydride is located between Ni and Fe. According to our calculations, in reaction with the ferrocenium ion, electron transfer occurs from the NiFe hydride complex to the ferrocenium ion, followed by a hydrogen atom transfer (HAT) to the second ferrocenium ion. The oxidation state of Fe varies during the redox process, different from the case of NiFe hydrogenase, where the oxidation state of Ni varies. A single-step hydride transfer occurs in the presence of a 10-methylacridinium ion (AcrH + ), which is more kinetically feasible than the HAT process. In contrast to the HAT and hydride-transfer process, the proton transfer occurs through a low barrier from a protonated diethyl ether. The revealed reaction mechanism guides the interpretation of the catalytic cycle of NiFe hydrogenase and leads to the development of efficient biomimetic catalysts for H 2 generation and an electron/hydride transfer.

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Section: Introductionmentioning

confidence: 99%

Electron and Hydride Transfer in a Redox-Active NiFe Hydride Complex: A DFT Study

et al. 2018

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“…[21] Len's former Honours student David Schilter presents nickel-iron hydrogenase models featuring redox active ligands, work which was conducted in Korea. [22] Former Lindoy postdoc Feng Li (Western Sydney University) presents the complexation behaviour of N 4 O 2 hexadentate Schiff-base ligands towards 3d metal ions. [23] Len's former Master's student Jon Beves (UNSW) and Ph.D. student Jason Price report on the use of hydrogen bonding of ruthenium(II) terpyridine complexes for crystal engineering.…”

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confidence: 99%