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Showing 1–10 of 10 results
Advanced filters: Author: Linus O. Johannissen Clear advanced filters

  • Crystal structures of cyanobacterial protochlorophyllide oxidoreductases reveal the basis of the photocatalytic activities of this enzyme, through the role of its active site in enabling the light-driven reduction of protochlorophyllide.

    • Shaowei Zhang
    • Derren J. Heyes
    • Nigel S. Scrutton
    Research
    Nature
    Volume: 574, P: 722-725

  • CarH is a bacterial B12-binding photoreceptor involved in transcriptional regulation. Here, the authors provide insights into B12 dynamics and associated cobalt redox changes following light activation. These demonstrate the CarH response integrates light and oxygen sensing.

    • Harshwardhan Poddar
    • Ronald Rios-Santacruz
    • David Leys
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • Photoreceptor proteins utilise biological chromophores to regulate a large range of cellular processes in response to light. Here the authors identify and characterise a sub-family of multi-centre photoreceptors, termed photocobilins, that not only utilise B12 but also contain biliverdin (BV) as an additional chromophore.

    • Shaowei Zhang
    • Laura N. Jeffreys
    • Nigel S. Scrutton
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • 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

  • Coenzyme B12 traditionally acts as cofactor to light-independent metabolic enzymes in bacteria and humans. Here, Kutta et al.present a time-resolved photochemical description of a B12-dependent photoreceptor protein, which represents a mechanistic foundation for B12 photobiology.

    • Roger J. Kutta
    • Samantha J. O. Hardman
    • Alex R. Jones
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-11

  • Light-dependent protochlorophyllide oxidoreductase (LPOR) is a light-activated enzyme that catalyses a vital step in chlorophyll biosynthesis and acts as a key regulator of plant greening. In this Review, the authors summarize recent progress in the functional, chemical and structural understanding of LPOR photocatalysis in plants.

    • Derren J. Heyes
    • Shaowei Zhang
    • Nigel S. Scrutton
    Reviews
    Nature Plants
    Volume: 7, P: 268-276