Electroenzymatic C–C Bond Formation from CO<sub>2</sub>

Cai, Rong; Milton, Ross D.; Abdellaoui, Sofiène; Park, Terry; Patel, Janki J.; Alkotaini, Bassam

doi:10.1021/jacs.8b02319

Cited by 65 publications

(80 citation statements)

References 31 publications

(34 reference statements)

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“…Furthermore, N 2 fixation with artificial systems is still in its infancy and pertinent mechanistic questions can extracted from studies with semi-artificial enzyme-hybrids. Of further interest is also the continued exploration of the promiscuity of N 2 ases, which exhibit activity towards H 2 production 86 , CO 2 reduction to C 1 products 87 and even C-C coupling 88 .…”

Section: Photoreductive Reactionsmentioning

confidence: 99%

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

et al. 2018

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Semi-artificial photosynthetic systems aim to overcome the limitations of natural and artificial photosynthesis while providing an opportunity to investigate their respective functionality. The progress and studies of these hybrid systems is the focus of this forward-looking perspective. In this review, we discuss how enzymes have been interfaced with synthetic materials and employed for semiartificial fuel production. In parallel, we examine how more complex living cellular systems can be recruited for in vivo fuel production in an approach where inorganic nanostructures are hybridized with photosynthetic and non-photosynthetic microorganisms. Side-by-side comparisons reveal strengths and limitations of enzyme-and microorganism-based hybrid systems, and lessons extracted from studying enzyme-hybrids can be applied to investigations of microorganism-hybrid devices. We conclude by putting semi-artificial photosynthesis in the context of its own ambitions and discuss how it can help address the grand challenges facing artificial systems for the efficient generation of solar fuels and chemicals.

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Section: Photoreductive Reactionsmentioning

confidence: 99%

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

et al. 2018

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“…Supporting density functional theory (DFT) calculations led to the conclusion that the protonation of a M-H at the FeMo-co is the rate-limiting step of H 2 evolution (within the MoFe protein component). In 2018, Cai et al also employed this approach to investigate catalysis of the VFe protein for H + and CO 2 reduction [171]. In addition to unsubstituted cobaltocene, mono-cobaltocene ([Co(Cp)(CpCOOH)], E o ' = −0.79 V vs. SHE) and di-carboxy cobaltocene ([Co(CpCOOH) 2 ], E o ' = −0.65 V vs. SHE) derivatives were also investigated as electron mediators for the VFe protein.…”

Section: Electrochemical Methods For Electron Transfermentioning

confidence: 99%

Natural and Engineered Electron Transfer of Nitrogenase

Milton

2020

Chemistry

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As the only enzyme currently known to reduce dinitrogen (N2) to ammonia (NH3), nitrogenase is of significant interest for bio-inspired catalyst design and for new biotechnologies aiming to produce NH3 from N2. In order to reduce N2, nitrogenase must also hydrolyze at least 16 equivalents of adenosine triphosphate (MgATP), representing the consumption of a significant quantity of energy available to biological systems. Here, we review natural and engineered electron transfer pathways to nitrogenase, including strategies to redirect or redistribute electron flow in vivo towards NH3 production. Further, we also review strategies to artificially reduce nitrogenase in vitro, where MgATP hydrolysis is necessary for turnover, in addition to strategies that are capable of bypassing the requirement of MgATP hydrolysis to achieve MgATP-independent N2 reduction.

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“…Cobaltocene‐mediated electrocatalysis was subsequently adopted to facilitate H + and CO 2 reduction by MoFe and the alternative FeFe protein (producing H 2 as well as HCOO − ) . Further, cobaltocene‐mediated electrocatalysis with the alternative VFe protein (where two additional cobaltocene derivatives were also explored) demonstrated that C−C bond formation could be catalyzed forming ethene and propene from CO 2 reduction . When coupled with its Fe protein (and ATP hydrolysis), the VFe protein is known to catalyze C−C bond formation from CO reduction …”

Section: Recent Examples Of Enzymatic Electrochemistry For Small Molementioning

confidence: 99%

Recent Enzymatic Electrochemistry for Reductive Reactions

Cadoux

Milton

2020

ChemElectroChem

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Enzymatic electrochemistry is the coupling of oxidoreductase enzymes to electrodes, where electrons are transferred between the electrode and an enzyme's cofactor(s). In addition to enzymatic electrochemistry enabling mechanistic study [such as the determination of cofactor reduction potential(s)], enzymatic electrocatalysis also enables substrate reduction or oxidation by exploiting the catalytic properties of enzymes. This Minireview illustrates some recent examples, in which electrodes are coupled with enzymes that catalyze the reduction of substrates such as dinitrogen (N 2 ), carbon dioxide (CO 2 ) and protons (H + ), performed by metalloenzymes such as nitrogenases, formate dehydrogenases and hydrogenases. We review some strategies to achieve electron transfer (such as mediated and direct electron transfer), as well as some key results of recent studies.

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Electroenzymatic C–C Bond Formation from CO₂

Cited by 65 publications

References 31 publications

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

Natural and Engineered Electron Transfer of Nitrogenase

Recent Enzymatic Electrochemistry for Reductive Reactions

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Electroenzymatic C–C Bond Formation from CO2

Cited by 65 publications

References 31 publications

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

Interfacing nature’s catalytic machinery with synthetic materials for semi-artificial photosynthesis

Natural and Engineered Electron Transfer of Nitrogenase

Recent Enzymatic Electrochemistry for Reductive Reactions

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Product

Resources

About

Electroenzymatic C–C Bond Formation from CO₂