Dr. Mike Hough
Daresbury
Laboratory
Keckwick Lane, Daresbury
Warrington, Cheshire
WA4 4AD (UK)
E-mail:m.a.hough@dl.ac.uk
Tel:+44 1925 603625
Fax:+44 1925 603748
Profile
My
background is in physics, followed by a PhD in protein crystallography.
My
principal research interest is in the structure-function relationship in metalloproteins.
My major technique is protein crystallography, although I have some interest
in the use of solution X-ray scattering, XAFS and ESR spectroscopy as complementary
techniques.
I
am currently involved in the following projects:
Cytochrome P450s
I am studying the fundamental properties of cytochrome P450s in collaboration with Astex Technology, Cambridge (link to www.astex-technology.co.uk).
Superoxide Dismutase and Motor Neuron disease
Up to 90 different mutations in the antioxidant enzyme superoxide dismutase cause the inherited form of motor neuron disease. In collaboration with UCLA, University of Massachussetts Medical School and the University of Texas we are undertaking the characterisation and structure determination of these mutants.
Quantum chemistry
I am involved in collaborations with Daresbury CSE and external groups to use quantum mechanical calculations to simulate the properties of copper containing metalloproteins.
Publications
Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. Svetlana Antonyuk, Jennifer Stine Elam, Michael A. Hough, Richard W. Strange, Peter A. Doucette, Jorge A. Rodriguez. Lawrence J. Hayward, Joan Selverstone Valentine, P. John Hart and S. Samar Hasnain. (2005). Protein Science 14, 1201-1213.
Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Douchette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS and Hasnain SS, (2004). Proceedings of the National Academy of Science 101, (16), 5976-5981
Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase from Alcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants. Barrett ML, Harris RL, Antonyuk S, Hough MA, Ellis MJ, Sawers G, Eady RR and Hasnain SS, (2004) Biochemistry 43, (51), 16311-16319
Structure of Fully Reduced Bovine Copper, Zinc Superoxide Dismutase at 1.15 Å. Michael A Hough & S. Samar Hasnain. (2005) Structure with Folding and Design. 11(8). 937-946.
The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis. Richard W. Strange, Svetlana Antonyuk, Michael A. Hough, Peter A. Doucette, Jorge A. Rodriguez, P. John Hart, Lawrence J. Hayward, Joan S. Valentine and S. Samar Hasnain. (2003). Journal of Molecular Biology, 328 (4), 877-891.