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Heat-fueled enzymatic cascade for selective oxyfunctionalization of hydrocarbons.

ABSTRACT: Heat is a fundamental feedstock, where more than 80% of global energy comes from fossil-based heating process. However, it is mostly wasted due to a lack of proper techniques of utilizing the low-quality waste heat (<100 °C). Here we report thermoelectrobiocatalytic chemical conversion systems for heat-fueled, enzyme-catalyzed oxyfunctionalization reactions. Thermoelectric bismuth telluride (Bi₂Te₃) directly converts low-temperature waste heat into chemical energy in the form of H₂O₂ near room temperature. The streamlined reaction scheme (e.g., water, heat, enzyme, and thermoelectric material) promotes enantio- and chemo-selective hydroxylation and epoxidation of representative substrates (e.g., ethylbenzene, propylbenzene, tetralin, cyclohexane, cis-β-methylstyrene), achieving a maximum total turnover number of rAaeUPO (TTN_rAaeUPO) over 32000. Direct conversion of vehicle exhaust heat into the enantiopure enzymatic product with a rate of 231.4 μM h^-1 during urban driving envisions the practical feasibility of thermoelectrobiocatalysis.

SUBMITTER: Yoon J

PROVIDER: S-EPMC9243031 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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Heat-fueled enzymatic cascade for selective oxyfunctionalization of hydrocarbons.

Yoon Jaeho J Jang Hanhwi H Oh Min-Wook MW Hilberath Thomas T Hollmann Frank F Jung Yeon Sik YS Park Chan Beum CB

Nature communications 20220629 1

Heat is a fundamental feedstock, where more than 80% of global energy comes from fossil-based heating process. However, it is mostly wasted due to a lack of proper techniques of utilizing the low-quality waste heat (<100 °C). Here we report thermoelectrobiocatalytic chemical conversion systems for heat-fueled, enzyme-catalyzed oxyfunctionalization reactions. Thermoelectric bismuth telluride (Bi<sub>2</sub>Te<sub>3</sub>) directly converts low-temperature waste heat into chemical energy in the fo ...[more]

PMID: 35768427

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Project description:Single enzymatic cascade, ubiquitously found in cellular signaling networks, is a phosphorylation-dephosphorylation reaction cycle causing a transition between inactive and active states of a protein catalysed by kinase and phosphatase, respectively. Steady-state information processing ability of such a cycle (e.g., MAPK cascade) has been classified into four qualitatively different operating regimes, viz., hyperbolic (H), signal-transducing (ST), threshold-hyperbolic (TH) and ultrasensitive (U). These four regimes represent qualitatively different dose-response curves, that is, relationship between concentrations of input kinase (e.g., pMEK) and response activated protein (e.g., pERK). Regimes were identified using a deterministic model accounting for population-averaged behavior only. Operating regimes can be strongly influenced by the inherently present cell-to-cell variability in an ensemble of cells which is captured in the form of pMEK and pERK distributions using reporter-based single-cell experimentation. In this study, we show that such experimentally acquired snapshot pMEK and pERK distribution data of a single MAPK cascade can be directly used to infer the underlying operating regime even in the absence of a dose-response curve. This deduction is possible primarily due to the presence of a monotonic relationship between experimental observables RIQR, ratio of the inter-quartile range of the pERK and pMEK distribution pairs and RM, ratio of the medians of the distribution pair. We demonstrate this relationship by systematic analysis of a quasi-steady state approximated model superimposed with an input gamma distribution constrained by the stimulus strength specific pMEK distribution measured on Jurkat-T cells stimulated with PMA. As a first, we show that introduction of cell-to-cell variability only in the upstream kinase achieved by superimposition of an appropriate input pMEK distribution on the dose-response curve can predict bimodal response pERK distribution in ST regime. Implementation of the proposed method on the input-response distribution pair obtained in stimulated Jurkat-T cells revealed that while low-dosage PMA stimulation preserves the H regime observed in resting cells, high-dosage causes H to ST regime transition.

Dataset Information

Heat-fueled enzymatic cascade for selective oxyfunctionalization of hydrocarbons.

Publications

Heat-fueled enzymatic cascade for selective oxyfunctionalization of hydrocarbons.

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