Oxidoreductases are enzymes that catalyze transfer of electrons from a donor (reductant) to an acceptor (oxidant) molecule, generally using nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD+) as cofactors. The name of the oxidoreductase generally takes the form of '[acceptor name] dehydrogenase'.

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  • News & Views |

    Conventional experiments for generating proteins with improved properties by directed evolution are iterative, lengthy and costly. Now, a label-free assay has been developed for ultrahigh-throughput microfluidic screening that can dramatically accelerate the discovery of superior biocatalysts from a single round of genetic randomization.

    • Wolf-Dieter Fessner
    Nature Catalysis 2, 738-739
  • News & Views |

    Hydrogenases are very powerful biocatalysts for dihydrogen cleavage. Now, X-ray crystallography shows how [Fe]-hydrogenase requires ligand exchanges at the metal centre and significant molecular motions to open and close its active site to effectively transfer a hydride to an electrophilic organic substrate.

    • Yvain Nicolet
    Nature Catalysis 2, 481-482
  • News & Views |

    High-yield production of a functionally active mimic of particulate methane monooxygenase in Escherichia coli has been presented. Investigation of its catalytic mode clarifies the role of duroquinol in biomimetic methanol production.

    • Sunney I. Chan
    •  & Steve S.-F Yu
    Nature Catalysis 2, 286-287
  • News & Views |

    The diversity of engineered amine dehydrogenases for reductive amination remains limited. Now, native amino dehydrogenases offering a different sequence space and catalytic features are discovered — enhancing and broadening the biocatalysis toolbox.

    • Andreas S. Bommarius
    Nature Catalysis 2, 288-289