FH
Dr. Florence J Hardy
University of Manchester, University of Washington, University of Oxford
Research areas: Biochemistry, Genetics and Molecular Biology · Molecular Biology · Enzyme Catalysis and Immobilization · Protein Structure and Dynamics · Metal-Catalyzed Oxygenation Mechanisms
Employment
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University of Manchester Lecturer in Chemical Biology2026 - Present
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University of Washington Post Doctoral Research Scholar2024 - 2026
- 2022 - 2024
Education
- 2018 - 2022
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University of Oxford MChem2012 - 2016
Projects & Funding
Projects & funding information is unavailable.
Publications (24)
- Design of enantioselective photoenzymes by scaffolding mirror image catalytic sites Save
- Atomic Functional Site Scaffolding in Biopolymers with RFdiffusion3 Save
- From First Principles to Function: How AI Is Reshaping Enzyme Design Save
- Efficient and selective energy transfer photoenzymes powered by visible light Save
- Photosensitizer Repositioning Affords an Enantiocomplementary Enzyme for [2+2]‐Cycloadditions Save
- Engineered enzymes for enantioselective nucleophilic aromatic substitutions Save
- Probing Ferryl Reactivity in a Nonheme Iron Oxygenase Using an Expanded Genetic Code Save
- Noncanonical Amino Acids in Biocatalysis Save
- A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme Save
- Building Enzymes through Design and Evolution Save
- Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase Save
- Engineering Mutually Orthogonal PylRS/tRNA Pairs for Dual Encoding of Functional Histidine Analogues Save
- A Non-Canonical Nucleophile Unlocks a New Mechanistic Pathway in a Designed Enzyme Save
- A Designed Photoenzyme for Enantioselective [2+2]-Cycloadditions Save
- Directed evolution of an efficient and thermostable PET depolymerase Save
- A Designed Photoenzyme Promotes Enantioselective [2+2]-Cycloadditions via Triplet Energy Transfer Save
- A Designed Photoenzyme Promotes Enantioselective [2+2]-Cycloadditions via Triplet Energy Transfer Save
- Directed Evolution of an Efficient and Thermostable PET Depolymerase Save
- The histidine-brace active site of a copper monooxygenase is redox active and forms part of an in-built enzyme repair mechanism Save
- A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase Save