An Artificial [Fe4S4]-Containing Metalloenzyme for the Reduction of CO2 to Hydrocarbons

Waser, Valérie; Mukherjee, Manjistha; Tachibana, Ryo; Igareta, Nico V.; Ward, Thomas R.

doi:10.1021/jacs.3c03546

Cited by 11 publications

(2 citation statements)

References 69 publications

(108 reference statements)

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“…CO binding to an [Fe 4 S 4 ] + cluster induces electron delocalization with a neighboring Fe site, resulting in a mixedvalent Fe 1.5+ Fe 2.5+ pair, thus enabling the activation of C-O bonds without highly negative redox states (Brown et al, 2022). Metalloproteins with Fe 4 S 4 clusters catalyze CO and CO 2 reduction to hydrocarbons (alkanes/alkenes) (Lee et al, 2010;Rebelein et al, 2015;Waser et al, 2023), significant in context of early Earth's life origins. Pyruvate is a central metabolite in Archaea, Bacteria and Eukarya kingdoms, where iron-sulfur enzymes connect pyruvate to carbon fixation pathways and thioester biochemistry (De Duve, 1991;Berg et al, 2010).…”

Section: The Relevance Of Inorganic Oxidoreductase Activity In Biolog...mentioning

confidence: 99%

Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology

Huang,

Harmer,

Schenk

et al. 2024

Front. Chem.

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Oxidoreductases play crucial roles in electron transfer during biological redox reactions. These reactions are not exclusive to protein-based biocatalysts; nano-size (<100 nm), fine-grained inorganic colloids, such as iron oxides and sulfides, also participate. These nanocolloids exhibit intrinsic redox activity and possess direct electron transfer capacities comparable to their biological counterparts. The unique metal ion architecture of these nanocolloids, including electron configurations, coordination environment, electron conductivity, and the ability to promote spontaneous electron hopping, contributes to their transfer capabilities. Nano-size inorganic colloids are believed to be among the earliest ‘oxidoreductases’ to have ‘evolved’ on early Earth, playing critical roles in biological systems. Representing a distinct type of biocatalysts alongside metalloproteins, these nanoparticles offer an early alternative to protein-based oxidoreductase activity. While the roles of inorganic nano-sized catalysts in current Earth ecosystems are intuitively significant, they remain poorly understood and underestimated. Their contribution to chemical reactions and biogeochemical cycles likely helped shape and maintain the balance of our planet’s ecosystems. However, their potential applications in biomedical, agricultural, and environmental protection sectors have not been fully explored or exploited. This review examines the structure, properties, and mechanisms of such catalysts from a material’s evolutionary standpoint, aiming to raise awareness of their potential to provide innovative solutions to some of Earth’s sustainability challenges.

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Section: The Relevance Of Inorganic Oxidoreductase Activity In Biolog...mentioning

confidence: 99%

Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology

Huang,

Harmer,

Schenk

et al. 2024

Front. Chem.

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show abstract

“…Similarly, CO binding to an [Fe 4 S 4 ] + cluster induces electron delocalization, enabling the activation of C–O bonds without highly negative redox states. 411 Metalloproteins containing Fe 4 S 4 clusters can catalyze the reduction of CO and CO 2 to hydrocarbons, 412 , 413 , 414 which is significant in the context of Earth’s early life.…”

Section: Bridge Of Inorganic Nanoparticles In Biomolecular Evolutionmentioning

confidence: 99%

Unveiling the role of inorganic nanoparticles in Earth’s biochemical evolution through electron transfer dynamics

Huang

2024

iScience

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In Vivo Synthetic Anticancer Approach by Resourcing Mouse Blood Albumin as a Biocompatible Artificial Metalloenzyme

Imai,

Muguruma,

Nakamura

et al. 2024

Angewandte Chemie

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Methods for producing drugs directly at the cancer site, particularly using bioorthogonal metal catalysts, are being explored to mitigate the side effects of therapy. Albumin‐based artificial metalloenzymes (ArMs) catalyze reactions in living mice while protecting the catalyst in the hydrophobic pocket. Here, we describe the in situ preparation and application of biocompatible tumor‐targeting ArMs using circulating albumin, which is abundant in the bloodstream. The ArM was formed using blood albumin through the intravenous injection of ruthenium conjugated with an albumin‐binding ligand; the tumor‐targeting unit was conjugated to the ArM using its catalytic activity, and the ArM was transported to the cancer site. The delivered ArM catalyzed a second tagging reaction of the proapoptotic peptide on the cancer surface, successfully suppressing cancer proliferation. This approach, which efficiently leveraged the persisting reactivity twice in vivo, holds promise for future in vivo metal‐catalyzed drug synthesis utilizing endogenous albumin.

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An Artificial [Fe₄S₄]-Containing Metalloenzyme for the Reduction of CO₂ to Hydrocarbons

Cited by 11 publications

References 69 publications

Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology

Inorganic Fe-O and Fe-S oxidoreductases: paradigms for prebiotic chemistry and the evolution of enzymatic activity in biology

Unveiling the role of inorganic nanoparticles in Earth’s biochemical evolution through electron transfer dynamics

In Vivo Synthetic Anticancer Approach by Resourcing Mouse Blood Albumin as a Biocompatible Artificial Metalloenzyme

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