Undergraduate Advisor (Biology)
Bachelor of Science (BS) Wuhan, PRC, Master of Science (MS) Academia Sinica, Beijing, Doctor of Philosophy (PhD) Philipps, Germany
Telephone: (519) 888-4567 ext. 33562
Office: Biology 1 379C
Physiology and enzymology of hyperthermophilic microorganisms. View available graduate positions (PDF). Current research interests: sulfur reduction and energy metabolism; thermostable dehydrogenases; alcohol metabolism; electron transfer and flavoproteins; enzyme evolution and protein engineering.
Hyperthermophiles are a group of microorganisms isolated mainly from deep sea hydrothermal vents and growing at temperatures above 90°C. The majority of hyperthermophiles are classified as Archaea that are considered as the most slowly evolving of all microorganisms. The metabolism at such high temperature (>100°C) raises many biochemical questions: how are biomolecules stabilized? are there new metabolic pathways and novel metabolites? do these pathways contain unusual enzymes with yet unknown catalytic mechanisms? what is the relationship between structure and function of biomolecules that evolved under extreme conditions? Answering these questions will provide valuable insight into high temperature biochemistry and protein engineering.
- Ying, X and Ma, K. 2011. Characterization of a Zinc-containing Alcohol Dehydrogenase with Stereoselectivity from Hyperthermophilic Archaeon Thermococcus guaymasensis. J. Bacteriol. 193:3009-3019.
- Yang, X. and K. Ma. 2010. Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 192: 1370–1376.
- Ying, X., A. M. Grunden, L. Nie, M. W.W. Adams and K. Ma. 2009. Molecular Characterization of the Recombinant Iron-Containing Alcohol Dehydrogenase from the Hyperthermophilic Archaeon, Thermococcus Strain ES1. Extremophiles. 13:299-311.
- Yang, X. and K. Ma. 2007. Characterization of an exceedingly active NADH oxidase from anaerobic hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 189:3312-3317.
- Ying, X., Y. Wang, H. R. Badiei , V. Karanassios, and K. Ma. 2006. Purification and Characterization of an iron-containing alcohol dehydrogenase from Extremely Thermophilic Bacterium Thermotoga hypogea. Arch. Microbiol. 187:499-510.
- Yang, X. and K. Ma. 2005. Purification and characterization of an NADH oxidase from extremely thermophilic anaerobic bacterium Thermotoga hypogea. Arch. Microbiol. 183:331-337.
- Yang, X. and K. Ma. 2005. Determination of hydrogen peroxide generated by reduced nicotinamide adenine dinucleotide oxidase. Anal. Biochem. 344:130-134.
- Hao, X.-L. and K. Ma. 2003. Minimal sulfur requirement for growth and sulfur-dependent metabolism of the hyperthermophilic archaeon Staphylothermus marinus. Archaea. 1:191-197.
- Srinivasan, V., K. Ma, M. W. W. Adams, M. G. Newton, J. Rose, and B.-C. Wang. 2002. Towards the crystal structure of glycerol dehydrogenase from Thermotoga maritima. Acta Crystallogr. D. Biol. Crystallogr. 58:867-869.
- Ma, K., M.W.W. Adams. 2001. Hydrogenase I and II from Pyrococcus furiosus. Methods in Enzymology. 331:208-216.
- Ma, K., M.W.W. Adams. 2001. Alcohol dehydrogenases from Thermococcus litoralis and Thermococcus strain ES-1. Methods in Enzymology. 331:195-201.
- Ma, K., M.W.W. Adams. 2001. NAD(P)H:rubredoxin oxidoreductase from Pyrococcus furiosus. Methods in Enzymology. 334:55-62.
- Ma, K., M.W.W. Adams. 2001. Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus. Methods in Enzymology. 334:40-45.
- Ma, K., R. Weiss, M. W. W. Adams. 2000. Characterization of sulfhydrogenase II from the hyperthermophilic Archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J. Bacteriol. In Press.
- Britton, K. L., K. S. P. Yip, S.E. Sedelnikova, T. J. Stillman, M. W. W. Adams, K. Ma, D. L. Meader, F. T. Robb, N. Tolliday, C. Vetriani, D. W. Rice and P. J. Baker. 2000. Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus. J. Mol. Biol. In Press.
- Ma, K. and Adams, M. W. W. 1999. A hyperactive NAD(P)H:rubredoxin oxidoreductase from hyperthermophilic Archaeon, Pyrococcus furiosus. J. Bacteriol. 181:5530-5534.
- Ma, K. and Adams, M. W. W. 1999. An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus. J. Bacteriol. 181:1163-1170.
- Ma, K., Hutchins, A., Sung, S.-J. S. and Adams, M. W. W. 1997. Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a coenzyme A-dependent pyruvate decarboxylase. Proc. Natl. Acad. Sci. USA. 94:9608-9613.
- Sedelnikova, S. E., Yip, K. S. P., Stillman, T.J., Ma, K., Adams, M.W.W., Robb, F.T. and Rice, D.W. 1996. Crystallization of the glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis. Acta Crystallographica Section D - Biological Crystallography.52(6):1185-1187.
- Ma, K., Loessner, H., Heider, J., Johnson, M. K. and Adams, M.W.W. 1995. Effects of elemental sulfur on the metabolism of the deep sea hyperthermophilic archaeon, Thermococcus strain ES-1: Purification and characterization of a novel, sulfur-regulated, non-heme iron alcohol dehydrogenase. J. Bacteriol., 177:4748-4756.
- Gorst, C. M., Zhou, Z.-H., Ma, K., Teng, Q., Howard, J. B., Adams, M. W.W. and La Mar, G. N. 1994. The participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H NMR time resolution of the four redox states at ambient temperatures. Biochemistry, 34:8788-8795.
- Ma, K., and Adams, M.W.W. 1994. Sulfide dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J. Bacteriol., 176:6509-6517.
- Ma, K., Schicho, R.N., Kelly, R.M., and Adams, M.W.W. 1993. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA, 90:5341-5344.