F. Scott Mathews, Ph.D.
Professor Emeritus
Biochemistry and Molecular Biophysics
Cell Biology and Physiology
Molecular Biophysics Program
Biochemistry Program
|  |
Office Phone: 314-362-1080
Lab Phone: 314-362-1079
Other Phone:
FAX: 314-362-7183
Box: 8231
Lab Address: 2911-D South Building
Email: mathews22@wustl.edu
Keywords: structural biology; protein structure; biophysics; oxidation reduction; electron transfer
Short Research Description: X-ray structure analysis of macromolecules. |
Research Abstract:
The laboratory is engaged in protein structure analysis by X-ray crystallography. The overall aim of this research is to learn how the structure of an enzyme determines its chemical and physiological properties.
Most of the enzymes being studied are involved in oxidation-reduction reactions and contain redox active cofactors. These generally fall into two classes, quinoenzymes and flavoenzymes. Four quinoprotein systems are being studied, a copper amine oxidase containing topaquinone, an alcohol dehydrogenase containing pyrroloquinolinequinone and two amine dehydrogenases, one containing tryptophan tryptophylquinone and the other cysteine tryptophylquinone. The flavoprotein systems are an iron-sulfur flavoprotein, an α-hydroxyacid oxidizing enzyme and a family of FAD-containing secondary amine oxidases. Crystallographic studies are underway to investigate substrate and inhibitor binding as well as mutant forms of these enzymes. In some cases we are also studying interactions of the redox enzymes with small electron carrier proteins.
The physical and chemical techniques used in this laboratory include protein purification and crystallization, x-ray diffraction, computer graphics and molecular biology. A rapid X-ray data acquisition system and several molecular graphics work stations are available. |
Selected Publications:
Sukumar N, Dewanti AR, Mitra B, Mathews FS. High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase. J Biol Chem 2004 279:3749-3757.
Xia ZX, Dai WW, He YN, et al. X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i. J Biol Inorg Chem 2003 8:843-854.
Chen ZW, Matsushita K, Yamashita T, et al. Structure at 1.9: A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. Structure 2002 10:837-849.
Zhao G, Song H, Chen ZW, et al. Monomeric sarcosine oxidase: Role of histidine 269 in catalysis. Biochemistry 2002 41:9751-9764.
Datta S, Mori Y, Takagi K, et al. Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking. Proc Natl Acad Sci USA 2001 98:14268-14273. |