Category: Mathews Publications

Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by NikD, an unusual amino acid oxidase.

Kommoju P.R., Bruckner R.C., Ferreira P., Carrell C.J., Mathews F.S., & Jorns M.S. (2009). “Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by NikD, an unusual amino acid oxidase.” Biochemistry. 2009 Oct 13;48(40):9542-55. doi: 10.1021/bi901056a. (Abstract)

Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.

Sukumar N., Dewanti A., Merli A., Rossi G.L., Mitra B., & Mathews F.S. (2009). “Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates.” Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):543-52. doi: 10.1107/S0907444909010270. Epub 2009 May 15. (Abstract)

Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis.

Sukumar N., Chen Z.W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A., Davidson V.L., & Mathews F.S. (2006). “Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis.” Biochemistry. 2006 Nov 14;45(45):13500-10. (Abstract)

Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated.

Ma J.K., Carrell C.J., Mathews F.S., & Davidson V.L. (2006). “Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated.” Biochemistry. 2006 Jul 11;45(27):8284-93. (Abstract)

High resolution crystal structures of free thrombin in the presence of K(+) reveal the molecular basis of monovalent cation selectivity and an inactive slow form.

Carrell C.J., Bush L.A., Mathews F.S., & Di Cera, E. (2006). “High resolution crystal structures of free thrombin in the presence of K(+) reveal the molecular basis of monovalent cation selectivity and an inactive slow form.” Biophys Chem. 2006 Jun 1;121(3):177-84. Epub 2006 Feb 17. (Abstract)