Rowena Green Matthews
Rowena Green Matthews is G. Robert Greenberg Distinguished University Professor Emeritus at the University of Michigan, Ann Arbor.[2] Her research focuses on the role of organic cofactors as partners of enzymes catalyzing difficult biochemical reactions, especially folic acid and cobalamin (vitamin B12). She is a Fellow of the National Academy of Sciences (elected 2002),[3] the Institute of Medicine (elected 2004),[4] the American Academy of Arts and Sciences (2005), the American Philosophical Society (2009) [5] and the American Academy of Microbiology (2002).
Early life and education
Matthews earned her B. A. in Biology, summa cum laude, from Radcliffe College in 1960. As an undergraduate, and for three years thereafter, she worked with George Wald and published a first author paper in which she first described a new intermediate in the bleaching of the visual pigment rhodopsin that temporally coincided with initiation of visual excitation.[6] She then went to graduate school in Biophysics at the University of Michigan, where she did her dissertation research in the laboratory of Vincent Massey. She received her Ph.D. in 1969.
Family
Matthews is the daughter of David E. Green and Doris Cribb Green. Her father was Professor of Biochemistry at the University of Wisconsin and was elected to the National Academy of Sciences in 1962. She married Larry Stanford Matthews in 1960, and they have two children, Brian and Keith, and two grandchildren, Jennifer and David. Her niece, Tammy Baldwin, is the junior Senator from Wisconsin, elected in 2012.
Career
Matthews did her postdoctoral research with Charles H. Williams, Jr. at the University of Michigan, and in 1978 she joined the faculty at Michigan as an Assistant Professor of Biological Chemistry. She has remained at Michigan throughout her academic career. She has published more than 100 papers in scientific journals, and trained many graduate students and postdoctoral fellows. She is the recipient of the William C. Rose Award of the American Society of Biochemistry and Molecular Biology (2000) and the Repligen Corporation Award in Chemistry of Biological Processes of the Division of Biological Chemistry of the American Chemical Society (2001).
She was the Frederick Gowland Hopkins Lecturer at 12th International Conference of Pteridines and Folates.[7] She currently serves on the Medical Advisory Board of the Howard Hughes Medical Institute,[8] and on the Council of the National Academy of Sciences.[9] She is a member of the American Philosophical Society.[10]
Publications
- Matthews, R. G.; Hubbard, R.; Brown, P. K.; Wald, G. (1963). "Tautomeric forms of metarhodopsin". Journal of General Phyhsiology 47: 215–240. doi:10.1085/jgp.47.2.215. PMC 2195338. PMID 14080814.
- Daubner, S. C.; Matthews, R. G. (1982). "Purification and properties of methylenetetrahydrofolate reductase from pig liver". Journal of Biological Chemistry 257 (1): 140–145.
- Banerjee, R. V.; Johnston, N. L.; Sobeski, J. K.; Datta, P.; Matthews, R. G. (1989). "Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tropic fragment containing the cobalamin-binding domain". Journal of Biological Chemistry 264 (23): 13888–13895.
- Goyette, P.; Sumner, J. S.; Milos, R.; Duncan, A. M. V.; Rosenblatt, D. S.; Matthews, R. G.; Rozen, R. (1994). "Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification". Nature Genetics 7: 195–200. doi:10.1038/ng0694-195. PMID 7920641.
- Frosst, P.; Blom, H. J.; Milos, R.; Goyette, P.; Sheppard, C. A.; Matthews, R. G.; Boers, G. J. H.; den Heijer, M.; Kluijtmans, L. A. J.; den Heuvel, L. P.; Rozen, R. (1995). "A candidate genetic risk factor for vascular disease: a common mutation in methyenetetrahydrofolate reductase". Nature Genetics 10: 111–113. doi:10.1038/ng0595-111. PMID 7647779.
- Drennan, C. L.; Huang, S.; Drummond, J. T.; Matthews, R. G.; Ludwig, M. L. (1994). "How a protein binds B12: a 3.0 Å x-ray structure of B12-binding domains of methionine synthase". Science 266: 1669–1674.
- González, J. C.; Peariso, K.; Penner-Hahn, J. E.; Matthews, R. G. (1996). "Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme". Biochemistry 35: 12228–12234. doi:10.1021/bi9615452. PMID 8823155.
- Ludwig, M. L.; Matthews, R. G. (1997). "Structure-based perspectives on B12-dependent enzymes". Ann. Rev. Biochem 66: 269–313. doi:10.1146/annurev.biochem.66.1.269. PMID 9242908.
- Goulding, C. W.; Postigo, D.; Matthews, R. G. (1997). "Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine". Biochemistry 36: 8082–8091. doi:10.1021/bi9705164.
- Goulding, C. W.; Matthews, R. G. (1997). "Cobalamin-dependent methionine synthase from Escherichia coli:involvement of zinc in homocysteine activation". Biochemistry 36: 15749–15757. doi:10.1021/bi971988l.
- Guenther, B. D.; Sheppard, C. A.; Tran, P.; Rozen, R.; Matthews, R. G.; Ludwig, M. L. (1999). "The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.". Nature Structural Biology 6: 359–365. doi:10.1038/7594.
- Bandarian, V.; Pattridge, K. A.; Lennon, B. W.; Huddler, D. P.; Matthews, R. G.; Ludwig, M. L. (2001). "Domain alteration switches B12-dependent methionine synthase to the activation conformation". Nature Structural Biology 9: 53–56. doi:10.1038/nsb738.
- Bandarian, V.; Ludwig, M. L.; Matthews, R. G. (2003). "Factors modulating conformational equilibria in large modular proteins: a case study with cobalamin-dependent methionine synthase". Proc. Natl. Acad. Sci. USA 100: 8156–8163. doi:10.1073/pnas.1133218100.
- Koutmos, M.; Pejchal, R.; Bomer, T. M.; Matthews, R. G.; Smith, J. L.; Ludwig, M. L. (2008). "Metal active site elasticity linked to activation of homocysteine in methionine synthases". Proc. Natl. Acad. Sci. USA 105: 3286–3291. doi:10.1073/pnas.0709960105.
- Matthews, R. G. (2009) Cobalamin- and corrinoid-dependent enzymes, in Metal Carbon Bonds in Enzymes and Cofactors, 6, Metal Ions in Life Sciences, Sigel, A., Sigel, H., and Sigel, R. K. O., eds. RSC Publishing, Cambridge UK, pp. 53–114.
- Koutmos, M.; Datta, S.; Pattridge, K. A.; Smith, J. L.; Matthews, R. G. (2009). "Insights into the reactivation of cobalamin-dependent methionine synthase". Proc. Natl. Acad. Sci. USA 106: 18527–18532. doi:10.1073/pnas.0906132106.
References
- ↑ Matthews, Rowena G.; Ruth Hubbard; Paul K. Brown; George Wald (1963). "Tautomeric forms of metarhodopsin". Journal of General Physiology 47: 215–240. doi:10.1085/jgp.47.2.215. PMC 2195338. PMID 14080814.
- ↑ Matthews, Rowena. "Rowena Matthews-University of Michigan Department of Biological Chemistry".
- ↑ Matthews, Rowena. "Rowena Matthews-National Academy of Sciences".
- ↑ Matthews, Rowena. "Directory: IOM Member-Rowena G. Matthews, Ph.D.". Global directory.
- ↑ Matthews, Rowena. "Institute News: American Philosophical Society Honors HHMI scientists and board members". American Philosophical Society.
- ↑ Matthews, Rowena G.; Ruth Hubbard; Paul K. Brown; George Wald (1963). "Tautomeric forms of metarhodopsin". Journal of General Physiology 47: 215–240. doi:10.1085/jgp.47.2.215. PMC 2195338. PMID 14080814.
- ↑ http://books.google.com/books?id=CvwnJmFmGcIC&pg=PR21&lpg=PR21&dq=Rowena+Green+Matthews&source=bl&ots=80jfeHTUpo&sig=tGZBm9tbdD3Q8xp6qFRyzEWBV0Y&hl=en&sa=X&ei=tjDHUtL-C864yAG4hYDgBQ&ved=0CDgQ6AEwBDgU#v=onepage&q=Rowena%20Green%20Matthews&f=false
- ↑ "Medical Advisory Board". Howard Hughes Medical Institute. Retrieved 25 March 2015.
- ↑ "Leadership and Governance". National Academy of Sciences. Retrieved 25 March 2015.
- ↑ http://www.amphilsoc.org/memhist/search?creator=Rowena+Matthews&title=&subject=&subdiv=&mem=&year=&year-max=&dead=&keyword=&smode=advanced