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Showing 1–6 of 6 results
Advanced filters: Author: Rebecca Crawshaw Clear advanced filters

  • Recent studies have shown that energy transfer photoenzymes can be engineered to promote stereocontrolled [2 + 2] cycloadditions; however, existing systems rely on ultraviolet light and display limited photochemical efficiencies. A generation of thioxanthone-containing photoenzymes now harnesses visible light to drive challenging photochemical conversions with high efficiencies and selectivities.

    • Rebecca Crawshaw
    • Ross Smithson
    • Anthony P. Green
    ResearchOpen Access
    Nature Chemistry
    Volume: 17, P: 1083-1090

  • A genetically encoded triplet photosensitizer is used to develop an efficient photoenzyme that can promote enantioselective intramolecular and bimolecular [2+2] cycloadditions by means of triplet energy transfer.

    • Jonathan S. Trimble
    • Rebecca Crawshaw
    • Anthony P. Green
    Research
    Nature
    Volume: 611, P: 709-714

  • The authors previously showed that a histidine nucleophile and a flexible arginine can work in synergy to accelerate the Morita Baylis-Hillman (MBH) reaction. Here, they report another efficient MBHase that employs a non-canonical Nδ-methylhistidine nucleophile paired with a catalytic glutamate, providing an alternative mechanistic solution for MBH catalysis.

    • Amy E. Hutton
    • Jake Foster
    • Anthony P. Green
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • Directed evolution of a primitive computationally designed enzyme has produced an efficient and enantioselective biocatalyst for the Morita–Baylis–Hillman reaction. The engineered enzyme uses a designed histidine nucleophile operating in synergy with a catalytic arginine that emerged during evolution and serves as a genetically encoded surrogate of privileged bidentate hydrogen-bonding catalysts.

    • Rebecca Crawshaw
    • Amy E. Crossley
    • Anthony P. Green
    Research
    Nature Chemistry
    Volume: 14, P: 313-320

  • A hydrolytic enzyme with a non-canonical organocatalytic mechanism was generated by introducing Nδ-methylhistidine into a designed active site using engineered translation components, allowing optimization of enzyme performance using laboratory evolution.

    • Ashleigh J. Burke
    • Sarah L. Lovelock
    • Anthony P. Green
    Research
    Nature
    Volume: 570, P: 219-223

  • Recent progress in computational enzyme design, active site engineering and directed evolution are reviewed, highlighting methodological innovations needed to deliver improved designer biocatalysts.

    • Sarah L. Lovelock
    • Rebecca Crawshaw
    • Anthony P. Green
    Reviews
    Nature
    Volume: 606, P: 49-58