Post-doctoral work: DFG Fellowship (2008-2012), Max-Planck for Biophysical Chemistry, Goettingen, Germany CEA Fellowship (2006-2008) at CEA-Saclay, France Postdoctoral research Associate (2003-2006), University of Denver, USA

The development and application of advanced electron paramagnetic resonance (EPR) techniques in the study of biomacromolecules. Sponsored by a Bruker UK Ltd. funded position and based at the national ESPRC EPR service we have a vast array of specialized instrumentation available to trap radical metabolites, probe the local environment of paramagnetic metal centres and measure distances between spin labels. We routinely use multifrequency continuous-wave (CW), double electron electron resonance (DEER), electron nuclear double resonance (ENDOR), hyperfine sublevel correlation spectroscopy (HYSCORE) and high-field EPR. A current focus is the development of commercial instrumentation to do transient EPR and the development of optically detected magnetic resonance (ODMR). Biological EPR We apply the latest EPR techniques to structural, mechanistic and kinetic questions concerning flavins, cytochromes, kinases, phosphatases and RNA binding proteins. In recent time, there has been a focus on studying the catalytic properties of peroxidase and P450 enzymes. Other expertise includes UV-vis stopped flow and rapid freeze-quench. Materials Science Given the prime location we also have a number of collaborations concerning novel materials. In all endeavours, we welcome collaborative partners both nationally and abroad. Phone calls always welcome. Industrial consulting, possible.

Casadei, C.M., Gumiero, A., Metcalfe, C.L., Murphy, E.J., Basran, J., Concilio, M.G., Teixeira, S.C.M. Schrader, Fielding, A.J., Ostermann, A., Blakeley, M.P., Raven, E.L.. Moody, P.C.E. Cryo-neutron crystallography captures the protonation state of ferryl heme in a peroxidase. Science. 2014 July; 345(6193): 193-197. eScholarID:229356 | DOI:DOI: 10.1126/science.1254398 Fielding, A.J.*, Concilio, M.G., Heaven, G., Hollas, M.A. New Developments in Spin Labels for Pulsed Dipolar EPR. Molecules. 2014; (19): 16998-17025. eScholarID:237873 | DOI:doi:10.3390/molecules191016998 Pievo, R., Angerstein, B., Fielding, A.J., Koch, C., Feussner, I., Bennati, M. A Rapid Freeze‐Quench Setup for Multi‐Frequency EPR Spectroscopy of Enzymatic Reactions. ChemPhysChem. 2013; 14(18): 4094-4101. eScholarID:215990 | DOI:10.1002/cphc.201300714 Koch, C., Tria, G., Fielding, A. J., Brodhun, F., Valerius, O., Feussner, K., Braus, G.H., Svergun, D.I., Bennati, M., Feussner, I. A structural model of PpoA derived from SAXS-analysis—Implications for substrate conversion. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2013 June; eScholarID:200578 | DOI:10.1016/j.bbalip.2013.06.003 Fielding, A.J.,* Parey, K., Ermler, U., Scheller, S., Jaun, B., Bennati, M. Advanced electron paramagnetic resonance on the catalytic iron–sulfur cluster bound to the CCG domain of heterodisulfide reductase and succinate: quinone reductase. Journal of Biological Inorganic Chemistry. 2013 October; eScholarID:208303 | DOI:10.1007/s00775-013-1037-x Pudney, C.R., Lane, R.S.K., Fielding, A.J., Magennis, S.W., Hay, S., Scrutton, N.S. Enzymatic single-molecule kinetic isotope effects. Journal of the American Chemical Society. 2013; 135(10): 3855-3864. eScholarID:193076 | DOI:10.1021/ja309286r

Koch, C., Fielding, A. J., Brodhun, F., Bennati, M.,Feussner, I. Linoleic acid positioning in psi factor producing oxygenase A, a fusion protein with an atypical cytochrome P450 activity. FEBS JOURNAL. 2012 May; 279(9): 1594-1606. eScholarID:162559 | DOI:10.1111/j.1742-4658.2011.08352.x