Welcome to the Miller Laboratory Web Pages 

Anne-Frances Miller

Professor of Chemistry, and of Biochemistry Download CV.

Send email.

The Miller group studies  Enzymatic Redox Catalysis  in the following areas.

1. Superoxide Dismutase Projects. The Fe-SOD and Mn-SOD of E. coli have been manipulated to produce variants with reduction midpoint potentials ranging over 0.9 V (21 kCal/mol or 89 kJ/mol), without disruption of the active site. Thus, this system serves as a molecular laboratory for modifying a non-heme-Fe site to perform desired chemistry. EPR and NMR spectroscopy, and Xray crystallography are used to explore the details of the mutant structures of these enzymes. Titrations of substrate analog binding, pH equilibria and redox equilibria provide quantitative measures of different fundamental elements of activity. Click here to learn more.  

2. Nitroreductase Projects. Nitroreductase is a promiscuous enzyme with promise for bioremediation of waste streams, explosives and biproducts of explosives. We are also developing it for converting inexpensive nitroaromatic compounds into the corresponding aromatic hydroxylamines and amines, which are invaluable starting materials for synthesis of pharmaceuticals. We have explored the basis for NR's promiscuity, which contrasts with dogma that each enzyme is selective for a given substrate. NMR reveals protein dynamics underlying NR's very broad substrate specificy range. Mechanistic studies also reveal an extremely simple mechanism depending primarily on the flavin and active site water molecules, and thus relatively independent of specific interactions with protein residues. Click here to learn more.

3. Solid-State NMR of Flavins. 15N and 13C NMR chemical shift tensors are sensitive probes of the natures and relative energies of the frontier orbitals: the very orbitals that underlie the flavin's reactivity.  Click here to learn more


Courses Download publication list. NMR Center Instructions for 15 NMR experiments Coming soon: Group Members

Partial update: August 2017                                                                                               

Copyright 2017 A.-F. Miller     

comments: A.-F. Miller