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Christina M. Payne
Researcher at University of Kentucky
Publications - 56
Citations - 2150
Christina M. Payne is an academic researcher from University of Kentucky. The author has contributed to research in topics: Cellulase & Glycoside hydrolase. The author has an hindex of 21, co-authored 53 publications receiving 1707 citations. Previous affiliations of Christina M. Payne include Royal College of Surgeons in Ireland & Oak Ridge National Laboratory.
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Journal ArticleDOI
Characterization and engineering of a two-enzyme system for plastics depolymerization.
Brandon C. Knott,Erika Erickson,Mark D. Allen,Japheth E. Gado,Rosie Graham,Fiona L. Kearns,Isabel Pardo,Ece Topuzlu,Jared J. Anderson,Harry P. Austin,Graham Dominick,Christopher W. Johnson,Nicholas A. Rorrer,Caralyn J. Szostkiewicz,Valérie Copié,Christina M. Payne,H. Lee Woodcock,Bryon S. Donohoe,Gregg T. Beckham,John McGeehan +19 more
TL;DR: The characterization of the MHETase enzyme and synergy of the two-enzyme PET depolymerization system may inform enzyme cocktail-based strategies for plastics upcycling and will inform future efforts in the biological deconstruction andUpcycling of mixed plastics.
Journal ArticleDOI
Crystal structure and computational characterization of the lytic polysaccharide monooxygenase GH61D from the basidiomycota fungus Phanerochaete chrysosporium
Miao Wu,Gregg T. Beckham,Gregg T. Beckham,Anna M. Larsson,Takuya Ishida,Seonah Kim,Christina M. Payne,Christina M. Payne,Michael E. Himmel,Michael F. Crowley,Svein Jarle Horn,Bjørge Westereng,Kiyohiko Igarashi,Masahiro Samejima,Jerry Ståhlberg,Vincent G. H. Eijsink,Mats Sandgren +16 more
TL;DR: The three-dimensional crystal structure of the basidiomycete Phanerochaete chrysosporium GH61D LPMO reveals a copper-bound active site common to LPMOs, a collection of aromatic and polar residues near the binding surface that may be responsible for regio-selectivity, and substantial differences in loop structures compared with other L PMO structures.
Journal ArticleDOI
Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to cellulose
Christina M. Payne,Michael G. Resch,Liqun Chen,Michael F. Crowley,Michael E. Himmel,Larry E. Taylor,Mats Sandgren,Jerry Ståhlberg,Ingeborg Stals,Ingeborg Stals,Zhongping Tan,Gregg T. Beckham,Gregg T. Beckham +12 more
TL;DR: Results suggest that glycosylated linkers in carbohydrate-active enzymes, which are intrinsically disordered proteins in solution, aid in dynamic binding during the enzymatic deconstruction of plant cell walls.
Journal ArticleDOI
Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity
Anna S. Borisova,Trine Isaksen,Maria Dimarogona,Abhishek A. Kognole,Geir Mathiesen,Anikó Várnai,Åsmund K. Røhr,Christina M. Payne,Christina M. Payne,Morten Sørlie,Mats Sandgren,Vincent G. H. Eijsink +11 more
TL;DR: The novel structure of NcLPMO9C enabled a comparative study, revealing that the oxidative regioselectivity of L PMO9s (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere.
Journal ArticleDOI
Harnessing glycosylation to improve cellulase activity.
Gregg T. Beckham,Ziyu Dai,James F. Matthews,Michelle Momany,Christina M. Payne,William S. Adney,Scott E. Baker,Michael E. Himmel +7 more
TL;DR: It is proposed that glycosylation, instead of hindering cellulase engineering, can be used as an additional tool to enhance enzyme activity, given deeper understanding of its molecular-level role in biomass deconstruction.