Category: Mathews Publications

Dr. F. Scott Mathews’ Publications

Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.

Sukumar N., Liu S., Li W., Mathews F.S., Mitra B., & Kandavelu P. (2018). “Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.” Biochimie. 2018 Jul 30. pii: S0300-9084(18)30212-8. doi: 10.1016/j.biochi.2018.07.017. (Abstract)

High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.

Chen Z.W., Vignaud C., Jaafar A., Levy B., Gueritte F., Guenard D., Lederer F., & Mathews F.S. (2012). “High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.” Biochimie. 2012 May;94(5):1172-9. doi: 10.1016/j.biochi.2012.02.003. Epub 2012 Feb 9. (Abstract)

Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate.

Kommoju P.R., Chen Z.W., Bruckner R.C., Mathews F.S., & Jorns, M.S. (2011). “Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate.” Biochemistry. 2011 Jun 21;50(24):5521-34. doi: 10.1021/bi200388g. Epub 2011 May 26. (Abstract)

The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase.

Li J., Gan J.H., Mathews F.S., & Xia Z.X. (2011). “The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase.” Biochem Biophys Res Commun. 2011 Mar 25;406(4):621-6. doi: 10.1016/j.bbrc.2011.02.107. Epub 2011 Feb 26. (Abstract)

Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface.

Choi M., Sukumar N., Mathews F.S., Liu A., & Davidson V.L. (2011). “Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface.” Biochemistry. 2011 Feb 22;50(7):1265-73. doi: 10.1021/bi101794y. Epub 2011 Jan 26. (Abstract)

Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.

Chen Z., Datta S., Dubois J.L., Klinman J.P., & Mathews F.S. (2010). “Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.” Biochemistry. 2010 Aug 31;49(34):7393-402. doi: 10.1021/bi100643y. (Abstract)

A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer.

Sukumar N., Mathews F.S., Langan P., & Davidson V.L. (2010). “A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer.” Proc Natl Acad Sci U S A. 2010 Apr 13;107(15):6817-22. doi: 10.1073/pnas.0912672107. Epub 2010 Mar 29. (Abstract)