E
Esther M. Johnston
Researcher at Stanford University
Publications - 11
Citations - 2021
Esther M. Johnston is an academic researcher from Stanford University. The author has contributed to research in topics: Active site & Electron transfer. The author has an hindex of 9, co-authored 11 publications receiving 1617 citations. Previous affiliations of Esther M. Johnston include University of York.
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Journal ArticleDOI
Copper Active Sites in Biology
Edward I. Solomon,David E. Heppner,Esther M. Johnston,Jake W. Ginsbach,Jordi Cirera,Munzarin F. Qayyum,Matthew T. Kieber-Emmons,Christian H. Kjaergaard,Ryan G. Hadt,Li Tian +9 more
TL;DR: This review presents in depth discussions of all these classes of Cu enzymes and the correlations within and among these classes, as well as the present understanding of the enzymology, kinetics, geometric structures, electronic structures and the reaction mechanisms these have elucidated.
Journal ArticleDOI
The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases
Kristian E. H. Frandsen,Thomas J. Simmons,Paul Dupree,Jens-Christian N. Poulsen,Glyn R. Hemsworth,Luisa Ciano,Esther M. Johnston,Morten Tovborg,Katja Salomon Johansen,Pernille von Freiesleben,Laurence Marmuse,Sébastien Fort,Sylvain Cottaz,Hugues Driguez,Bernard Henrissat,Bernard Henrissat,Bernard Henrissat,Nicolas Lenfant,Nicolas Lenfant,Floriana Tuna,Amgalanbaatar Baldansuren,Gideon J. Davies,Leila Lo Leggio,Paul H. Walton +23 more
TL;DR: A structural determination of an LPMO-oligosaccharide complex is reported, yielding detailed insights into the mechanism of action of these enzymes.
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Lytic Polysaccharide Monooxygenases in Biomass Conversion
TL;DR: LPMOs offer tremendous promise for further process improvements owing to their ability to boost the activity of biomass-degrading enzyme consortia, and the academic literature in this area is reviewed.
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QM/MM studies into the H2O2-dependent activity of lytic polysaccharide monooxygenases: evidence for the formation of a caged hydroxyl radical intermediate
Binju Wang,Esther M. Johnston,Pengfei Li,Pengfei Li,Sason Shaik,Gideon J. Davies,Paul H. Walton,Carme Rovira,Carme Rovira +8 more
TL;DR: It is shown that there is an efficient mechanism to break the O–O bond of H2O2, with a low barrier of 5.8 kcal/mol, via a one-electron transfer from the LPMO-Cu(I) site to form an HO• radical, stabilized by hydrogen bonding interactions.
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Structure–function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family
Delu Tyler Yin,Saioa Urresti,Mickael Lafond,Mickael Lafond,Esther M. Johnston,Fatemeh Derikvand,Luisa Ciano,Jean-Guy Berrin,Bernard Henrissat,Paul H. Walton,Gideon J. Davies,Harry Brumer +11 more
TL;DR: Rec recombinant production and detailed structure–function analyses of two homologues from the phytopathogenic fungi Colletotrichum graminicola and C. gloeosporioides are reported to explore the wider biocatalytic potential in AA5, highlighting the significant potential of prospecting the evolutionary diversity of AA5 to reveal novel enzyme specificities, thereby informing both biology and applications.