A. Gunn

发表

Evidence for a Two-Electron Transfer Using the All-Ferrous Fe Protein during Nitrogenase Catalysis*

G. Watt, A. Nyborg, Joseph L. Johnson, 2000, The Journal of Biological Chemistry.

Nitrogenase Reactivity Using Ti(III) as Reductant

G. Watt, A. Nyborg, Joseph L. Johnson, 2002 .

Reactions of Azotobacter vinelandii nitrogenase using Ti(III) as reductant.

J. Johnson, J. Erickson, G. Watt, 2000, Journal of inorganic biochemistry.

Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants that form the all-ferrous redox state of the Fe protein.

J. Johnson, J. Erickson, G. Watt, 1999, Biochemistry.

Conformationally distinct five-coordinate heme-NO complexes of soluble guanylate cyclase elucidated by multifrequency electron paramagnetic resonance (EPR).

M. Marletta, R. D. Britt, E. Derbyshire, 2012, Biochemistry.

Characterization of two different five-coordinate soluble guanylate cyclase ferrous-nitrosyl complexes.

M. Marletta, R. D. Britt, M. Ibrahim, 2008, Biochemistry.

Influence of Electromagnetic Fields on Nuclear Processes

C. Shih, Q. Wang, B. Mei, 2020, 2011.05385.

Multifrequency pulsed EPR studies of biologically relevant manganese(II) complexes

V. DeRose, R. D. Britt, T. A. Stich, 2007, Applied magnetic resonance.

Structure of the biliverdin radical intermediate in phycocyanobilin:ferredoxin oxidoreductase identified by high-field EPR and DFT.

A. Fisher, R. D. Britt, A. Ozarowski, 2009, Journal of the American Chemical Society.

Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants.

A. Fisher, R. D. Britt, T. Doukov, 2010, Biochemistry.

Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates.

R. D. Britt, M. Toney, J. Lagarias, 2004, Journal of the American Chemical Society.