M. J. Lavery

Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2[Fe4S4] ferredoxin from Clostridium pasteurianum.

M. Sadek, R. Brownlee, P. S. Brereton, 1994, Biochemistry.

The Rubredoxin from Clostridium pasteurianum: Mutation of the Conserved Glycine Residues 10 and 43 to Alanine and Valine

A. G. Wedd, K. Nugent, M. Ayhan, 1996 .

The Rubredoxin from Clostridium pasteurianum: Mutation of the Iron Cysteinyl Ligands to Serine. Crystal and Molecular Structures of Oxidized and Dithionite-Treated Forms of the Cys42Ser Mutant

M. Wilce, J. Guss, G. George, 1998 .

The dependence of reversible potentials on the form of modification of edge plane pyrolytic graphite electrodes in voltammetric studies on rubredoxin and ferredoxin from Clostridium pasteurianum

A. Bond, A. G. Wedd, M. J. Lavery, 1999 .