Zobrazeno 1 - 10
of 318
pro vyhledávání: '"FRASER A. ARMSTRONG"'
Publikováno v:
Communications Chemistry, Vol 7, Iss 1, Pp 1-11 (2024)
Abstract An emerging concept and platform, the electrochemical Leaf (e-Leaf), offers a radical change in the way tandem (multi-step) catalysis by enzyme cascades is studied and exploited. The various enzymes are loaded into an electronically conducti
Externí odkaz:
https://doaj.org/article/ecd9d20b4aea491f8e9368d1a01f0112
Autor:
Raphael Reinbold, Ingvild C. Hvinden, Patrick Rabe, Ryan A. Herold, Alina Finch, James Wood, Melissa Morgan, Maximillian Staudt, Ian J. Clifton, Fraser A. Armstrong, James S. O. McCullagh, Jo Redmond, Chiara Bardella, Martine I. Abboud, Christopher J. Schofield
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
The development of IDH variant inhibitors is a breakthrough as it is the first time metabolism has been successfully targeted by small molecule drugs in cancer. Here the authors report studies on resistance to the pioneer drug ivosidenib leading to i
Externí odkaz:
https://doaj.org/article/e3e859d6d730417f8d6ec356de38fe1b
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Multistep enzymatic reactions (cascades) can be achieved by confining enzymes in synthetic materials, but ways to simultaneously energize, control and observe the reactions in real time are lacking. Here, bidirectional interconversion between asparta
Externí odkaz:
https://doaj.org/article/91664833a62049bcaba7a424fead66f7
Publikováno v:
Biographical Memoirs of Fellows of the Royal Society. 73:471-497
Andrew Thomson developed and exploited optical and magnetic resonance spectroscopy to address unresolved questions in biological inorganic chemistry, in a career that spanned more than 50 years. Despite his important role in the discovery of cisplati
Publikováno v:
Chemical Communications. 58:11713-11716
The unique ability of the 'electrochemical leaf' (e-Leaf) to drive and control nanoconfined enzyme cascades bidirectionally, while directly monitoring their rate in real-time as electrical current, is exploited to achieve deracemisation and stereoinv
Publikováno v:
Chemical reviews.
Protein film electrochemistry (PFE) has given unrivalled insight into the properties of redox proteins and many electron-transferring enzymes, allowing investigations of otherwise ill-defined or intractable topics such as unstable Fe-S centers and th
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 120(1)
Isocitrate dehydrogenase 1 (IDH1) naturally copurifies and crystallizes in a resting state with a molecule of its exchangeable cofactor, NADP + /NADPH, bound in each monomer of the homodimer. We report electrochemical studies with IDH1 that exploit t
Autor:
Clare F. Megarity, Thomas R. I. Weald, Rachel S. Heath, Nicholas J. Turner, Fraser A. Armstrong
Publikováno v:
Megarity, C F, Weald, T R I, Heath, R S, Turner, N J & Armstrong, F A 2022, ' A Nanoconfined Four-Enzyme Cascade Simultaneously Driven by Electrical and Chemical Energy, with Built-in Rapid, Confocal Recycling of NADP(H) and ATP ', ACS Catalysis, vol. 12, no. 15, pp. 8811–8821 . https://doi.org/10.1021/acscatal.2c00999
The importance of energized nanoconfinement for facilitating the study and execution of enzyme cascades that feature multiple exchangeable cofactors is demonstrated by experiments with carboxylic acid reductase (CAR), an enzyme that requires both NAD
Autor:
Martine I. Abboud, Ryan A. Herold, Raphael Reinbold, Clare F. Megarity, Christopher J. Schofield, Fraser A. Armstrong
Publikováno v:
The Journal of Physical Chemistry Letters
Herold, R A, Reinbold, R, Megarity, C F, Abboud, M I, Schofield, C J & Armstrong, F A 2021, ' Exploiting Electrode Nanoconfinement to Investigate the Catalytic Properties of Isocitrate Dehydrogenase (IDH1) and a Cancer-Associated Variant ', Journal of Physical Chemistry Letters, vol. 12, pp. 6095-6101 . https://doi.org/10.1021/acs.jpclett.1c01517
Herold, R A, Reinbold, R, Megarity, C F, Abboud, M I, Schofield, C J & Armstrong, F A 2021, ' Exploiting Electrode Nanoconfinement to Investigate the Catalytic Properties of Isocitrate Dehydrogenase (IDH1) and a Cancer-Associated Variant ', Journal of Physical Chemistry Letters, vol. 12, pp. 6095-6101 . https://doi.org/10.1021/acs.jpclett.1c01517
Human isocitrate dehydrogenase (IDH1) and its cancer-associated variant (IDH1 R132H) are rendered electroactive through coconfinement with a rapid NADP(H) recycling enzyme (ferredoxin-NADP+ reductase) in nanopores formed within an indium tin oxide el
Autor:
Oliver Lampret, Martin Winkler, Jifu Duan, Thomas Happe, Fraser A. Armstrong, Eckhard Hofmann
Publikováno v:
Proc Natl Acad Sci U S A
As paradigms for proton-coupled electron transfer in enzymes and benchmarks for a fully renewable H(2) technology, [FeFe]-hydrogenases behave as highly reversible electrocatalysts when immobilized on an electrode, operating in both catalytic directio