“So, instead of having to analyze an entire protein, you can take a shortcut and focus your measurements just on the active site,” she continues. This “smart” DNP, as Miller refers to it, should make the technique more applicable than ever, as a researcher won’t need large quantities of protein or even a pure sample. Only protein molecules containing the flavin would be evident in a DNP-NMR spectrum.
Miller, A.-F. (2008) Redox Tuning Over Almost 1 V in a Structurally-conserved Active Site: Lessons from Superoxide Dismutase. Acc. Chem. Res. 41, 501-510.
Koder, R. L.,Walsh, J. D., Pometun, M. S., Dutton, P. L., Wittebort, R. J., and Miller, A.-F. (2006) 15N Solid-state NMR Provides a Sensitive Probe of Oxidized Flavin Reactive Sites. J. Am. Chem. Soc. 128, 15200–15208.
Vance, C. K. and Miller, A.-F. (1998) A Simple Proposal that can Explain the Inactivity of Metal-substituted Superoxide Dismutases. J. Am. Chem. Soc. 120, 461-467.
Miller, A.-F., Halkides, C. J., and Redfield, A. G. (1993) An NMR Comparison of the Changes Produced by Different Guanosine 5’-Triphosphate Analogs in Wild-type and Oncogenic Mutant p21ras. Biochemistry 32, 7367–7376.
Miller, A.-F. and Brudvig, G. W. (1989) Manganese and Calcium Requirements for Reconstitution of Oxygen-Evolution Activity in Manganese-Depleted Photosystem II Membranes. Biochemistry 28, 8181–8190.
Nick Zagorski (firstname.lastname@example.org) is a science writer at ASBMB.