A generalized kinetic model for compartmentalization of organometallic catalysis

Jolly, Brandon; Co, Nathalie; Davis, Ashton; Diaconescu, Paula L.; Liu, Chong

doi:10.1039/d1sc04983f

Cited by 7 publications

(5 citation statements)

References 61 publications

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“…In cases of catalyst poisoning, it is possible to design a compartment that addresses just that. 33 Liu and coworkers were able to create an anoxic microenvironment that prevents oxygen poisoning of the catalyst, yet still allowed O 2 to be used in the oxidation of methane to methanol (Fig. 2).…”

Section: Guiding Principlesmentioning

confidence: 99%

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The art of compartment design for synthetic catalysts

Davis

Liu

Diaconescu

2023

Inorg. Chem. Front.

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Section: Guiding Principlesmentioning

confidence: 99%

“…By introducing diffusion limitations, kinetic factors could be manipulated, something not possible to do in non-confined systems.In this instance, changing kinetic factors ultimately led to enhanced reaction rates and turnover numbers for the catalyst and, ultimately, being able to combine two otherwise incompatible reactions. 33…”

Section: Guiding Principlesmentioning

confidence: 99%

The art of compartment design for synthetic catalysts

Davis

Liu

Diaconescu

2023

Inorg. Chem. Front.

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“…Other models have been proposed, for example, one by Liu and co-workers , that addresses the flux of small organometallic catalyst molecules in and out of compartments; however, these models are less applicable to the case of immobilized enzyme cascades. Hinzpeter et al also used modeling methods to predict optimal compartment sizes and composition of the cascades within the compartment …”

Section: Nanoconfining and Energizing Enzyme Cascades For Technologymentioning

confidence: 99%

From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf

et al. 2022

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Protein film electrochemistry (PFE) has given unrivalled insight into the properties of redox proteins and many electron-transferring enzymes, allowing investigations of otherwise ill-defined or intractable topics such as unstable Fe–S centers and the catalytic bias of enzymes. Many enzymes have been established to be reversible electrocatalysts when attached to an electrode, and further investigations have revealed how unusual dependences of catalytic rates on electrode potential have stark similarities with electronics. A special case, the reversible electrochemistry of a photosynthetic enzyme, ferredoxin-NADP+ reductase (FNR), loaded at very high concentrations in the 3D nanopores of a conducting metal oxide layer, is leading to a new technology that brings PFE to myriad enzymes of other classes, the activities of which become controlled by the primary electron exchange. This extension is possible because FNR-based recycling of NADP(H) can be coupled to a dehydrogenase, and thence to other enzymes linked in tandem by the tight channelling of cofactors and intermediates within the nanopores of the material. The earlier interpretations of catalytic wave-shapes and various analogies with electronics are thus extended to initiate a field perhaps aptly named “cascade-tronics”, in which the flow of reactions along an enzyme cascade is monitored and controlled through an electrochemical analyzer. Unlike in photosynthesis where FNR transduces electron transfer and hydride transfer through the unidirectional recycling of NADPH, the “electrochemical leaf” (e-Leaf) can be used to drive reactions in both oxidizing and reducing directions. The e-Leaf offers a natural way to study how enzymes are affected by nanoconfinement and crowding, mimicking the physical conditions under which enzyme cascades operate in living cells. The reactions of the trapped enzymes, often at very high local concentration, are thus studied electrochemically, exploiting the potential domain to control rates and direction and the current–rate analogy to derive kinetic data. Localized NADP(H) recycling is very efficient, resulting in very high cofactor turnover numbers and new opportunities for controlling and exploiting biocatalysis.

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“…This success is driven by the fact that many of the obstacles that arise when implementing unusual chemistry in living systems are likely to be mitigated by new biochemical applications based on the extension of concepts such as those related to compartmentalization (Jolly et al, 2022). Indeed, a second major feature of local implementation of SynBio constructs is the recognition that many metabolites or precursors of important products of industrial interest are not compatible with each other, as they will have an inevitable tendency to react together.…”

Section: Sustainability‐driven Metabolic Engineeringmentioning

confidence: 99%

SynBio 2.0, a new era for synthetic life: Neglected essential functions for resilience

Danchin

Huang

2022

Environmental Microbiology

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A generalized kinetic model for compartmentalization of organometallic catalysis

Abstract: Compartmentalization is an attractive approach to enhance catalytic activity by retaining reactive intermediates and mitigating deactivating pathways. Such a concept has been well explored in biochemical and more recently, organometallic...

Cited by 7 publications

References 61 publications

The art of compartment design for synthetic catalysts

The art of compartment design for synthetic catalysts

From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf

SynBio 2.0, a new era for synthetic life: Neglected essential functions for resilience

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