Fraser Armstrong, Ph.D.
Affiliations: | Inorganic Chemistry Laboratory | University of Oxford, Oxford, United Kingdom |
Website:
http://research.chem.ox.ac.uk/fraser-armstrong.aspxGoogle:
"Fraser Armstrong"Bio:
http://armstrong.chem.ox.ac.uk/index.html
Mean distance: (not calculated yet) | S | N | B | C | P |
Cross-listing: Telomere and Telomerase Tree
Parents
Sign in to add mentor| A. Geoffrey Sykes | grad student | 1978 | University of Leeds |
| Helmut Beinert | post-doc | UW Madison | |
| H. Allen O. Hill | post-doc | Oxford |
Children
Sign in to add trainee| Bhavin Siritanaratkul | grad student | ||
| Anne Katherine Jones | grad student | 1998-2002 | Oxford |
| Sean J. Elliott | grad student | 2000-2002 | Oxford |
| Alison Parkin | grad student | 2004-2008 | Oxford |
| Michael J. Lukey | grad student | 2009-2013 | Oxford (Cell Biology Tree) |
| Sadagopan Krishnan | post-doc | Oxford | |
| Alison Parkin | post-doc | Oxford | |
| Kylie Vincent | post-doc | Oxford | |
| Yatendra S Chaudhary | post-doc | 2010-2012 | Oxford University UK |
| Erwin Reisner | research scientist | 2008-2009 | Oxford |
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Publications
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| Schmidt A, Kalms J, Lorent C, et al. (2023) Stepwise conversion of the Cys[4Fe-3S] to a Cys[4Fe-4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase. Chemical Science. 14: 11105-11120 |
| Evans RM, Beaton SE, Rodriguez Macia P, et al. (2023) Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' from . Chemical Science. 14: 8531-8551 |
| Herold RA, Reinbold R, Schofield CJ, et al. (2022) NADP(H)-dependent biocatalysis without adding NADP(H). Proceedings of the National Academy of Sciences of the United States of America. 120: e2214123120 |
| Armstrong FA, Cheng B, Herold RA, et al. (2022) From Protein Film Electrochemistry to Nanoconfined Enzyme Cascades and the Electrochemical Leaf. Chemical Reviews |
| Cheng B, Heath RS, Turner NJ, et al. (2022) Deracemisation and stereoinversion by a nanoconfined bidirectional enzyme cascade: dual control by electrochemistry and selective metal ion activation. Chemical Communications (Cambridge, England) |
| Ash PA, Kendall-Price SET, Evans RM, et al. (2021) The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase. Chemical Science. 12: 12959-12970 |
| Armstrong FA. (2021) Some fundamental insights into biological redox catalysis from the electrochemical characteristics of enzymes attached directly to electrodes. Electrochimica Acta. 390: 138836 |
| Herold RA, Reinbold R, Megarity CF, et al. (2021) Exploiting Electrode Nanoconfinement to Investigate the Catalytic Properties of Isocitrate Dehydrogenase (IDH1) and a Cancer-Associated Variant. The Journal of Physical Chemistry Letters. 12: 6095-6101 |
| Evans RM, Krahn N, Murphy BJ, et al. (2021) Selective cysteine-to-selenocysteine changes in a [NiFe]-hydrogenase confirm a special position for catalysis and oxygen tolerance. Proceedings of the National Academy of Sciences of the United States of America. 118 |
| Morello G, Megarity CF, Armstrong FA. (2021) The power of electrified nanoconfinement for energising, controlling and observing long enzyme cascades. Nature Communications. 12: 340 |