Rowena Green Matthews
Rowena Green Matthews | |
---|---|
![]() | |
Born | Rowena Green 1938 (age 85–86) |
Alma mater | University of Michigan |
Known for | Studies of cobalamin and folic acid |
Awards |
|
Scientific career | |
Fields | Biochemistry |
Institutions | University of Michigan |
Doctoral advisor | Vincent Massey |
Rowena Green Matthews, born in 1938,[1] is the 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). Among other honors, she was elected to the National Academy of Sciences in 2002 and the Institute of Medicine in 2004.[2]
Early life and education[edit]
Matthews was born in Cambridge, England while her father, biochemist David E. Green, was on sabbatical there.[3]: xxi Matthews earned her B.A. in biology summa cum laude from Radcliffe College in 1960.[4] As an undergraduate, and for three years thereafter, she worked with George Wald studying a new intermediate in the bleaching of the visual pigment rhodopsin that temporally coincided with initiation of visual excitation.[5] She then attended graduate school in biophysics at the University of Michigan, with dissertation research in the laboratory of Vincent Massey. She received her Ph.D. in 1969.[6]
Academic career[edit]
After finishing her Ph.D., Matthews remained at the University of Michigan as a postdoctoral fellow in the laboratory of Charles Williams in the department of Biological Chemistry and Assistant Research Scientist in the Biophysics Research Division in 1978. She was promoted to Associate Professor in 1981 became a full professor in 1986, and became the G. Robert Greenberg Distinguished University Professor in 1995.[2][6][7] In 2002, she assumed the position of Senior Research Professor and Charter Faculty Member of the Life Sciences Institute.[8] She retired in 2007, assuming professor emeritus status.[6]
Awards[edit]
She received numerous recognitions and honors during her career, the Repligen award given by the ACS (2001),[9] election to the National Academy of Sciences (2002),[10] the American Academy of Microbiology (2002),[2] the Institute of Medicine (2004),[11] the American Academy of Arts and Sciences (2005), and the American Philosophical Society (2009).[12][13] She received the William C. Rose Award given by the American Society for Biochemistry and Molecular Biology in 2000 and the Repligen Corporation Award in Chemistry of Biological Processes given by the American Chemical Society in 2001.[2]
She was the Frederick Gowland Hopkins Lecturer at 12th International Conference of Pteridines and Folates in 2001, an honor she particularly appreciated because her father had worked with Hopkins.[3] She serves on the Medical Advisory Board of the Howard Hughes Medical Institute,[14] and has served on the Council of the National Academy of Sciences.[15]
The University of Michigan hosts a professorship honoring Matthews; since 2009 James Bardwell has held the Rowena G. Matthews Collegiate Professorship.[16]
Research[edit]
Dr. Matthew's research focused on one-carbon metabolism, with particular emphasis on the enzymes that catalyze the de novo generation of methyl groups: methionine synthase, a B-12 dependent enzyme in humans, and methylenetetrahydrofolate reductase.[17][18] Her collaboration with geneticist Rima Rozen at McGill University led to the cloning of human methylenetetrahydrofolate reductase and the characterization of the C677T polymorphism associated with hyperhomocysteinemia in humans.[19][20] The polymorphism can lead to a high amount of homocysteine in the bloodstream. High concentrations of homocysteine in the plasma can increase the risk for cardiovascular diseases and the use of folic acid have been shown to decrease the amounts in humans.[21] In collaboration with Prof. Martha Ludwig they elucidated the first X-ray structure of vitamin B12 bound to a protein, cobalamin-dependent methionine synthase.[20][22]
Selected publications[edit]
- A love affair with vitamins (2009)[23]
- Cobalamin- and corrinoid-dependent enzymes[24]
- Cobalamin-dependent and cobamide-dependent methyltransferases (2008)[25]
Personal life[edit]
Matthews is the eldest daughter of biochemist David E. Green and the aunt of United States Senator Tammy Baldwin.[26]
References[edit]
- ^ "Rowena Green Matthews from Ann Arbor, Michigan | VoterRecords.com". voterrecords.com. Retrieved 2019-09-26.
- ^ Jump up to: a b c d e "Rowena Matthews, Ph.D." University of Michigan, Ann Arbor. 2014-08-13. Retrieved 3 August 2016.
- ^ Jump up to: a b Shane, Barry (2002). Milstein, Sheldon; Kapatos, Gregory; Levine, Robert A.; Shane, Barry (eds.). Chemistry and Biology of Pteridines and Folates Proceedings of the 12th International Symposium on Pteridines and Folates, National Institutes of Health, Bethesda, Maryland, June 17-22, 2001. Boston, MA: Springer US. ISBN 9781461509455.
- ^ "Tangs for the memories | Michigan Today". michigantoday.umich.edu. 20 September 2017. Retrieved 2019-09-26.
- ^ Matthews, Rowena G.; Ruth Hubbard; Paul K. Brown; George Wald (1963). "Tautomeric forms of metarhodopsin". Journal of General Physiology. 47 (2): 215–240. doi:10.1085/jgp.47.2.215. PMC 2195338. PMID 14080814.
- ^ Jump up to: a b c "Rowena Matthews". University of Michigan Faculty History Project. Retrieved 3 August 2016.
- ^ "Memoir | Faculty History Project". www.lib.umich.edu. Retrieved 2019-09-26.
- ^ "Emeritus Faculty". Life Sciences Institute. 2018-03-23. Retrieved 2019-09-26.
- ^ "Repligen Corporation Award in Chemistry of Biological Processes" (PDF). The Repligen Award.
- ^ Matthews, Rowena. "Rowena Matthews-National Academy of Sciences".
- ^ Matthews, Rowena. "Directory: IOM Member-Rowena G. Matthews, Ph.D." Global directory. Archived from the original on 2013-08-15.
- ^ "American Philosophical Society Honors HHMI Scientists and Board Members". HHMI News. 7 May 2009. Retrieved 7 August 2016.
- ^ "Dr. Rowena G. Matthews". American Philosophical Society Member History. Retrieved 7 August 2016.
- ^ "Medical Advisory Board". Howard Hughes Medical Institute. Retrieved 25 March 2015.
- ^ "Leadership and Governance". National Academy of Sciences. Retrieved 25 March 2015.
- ^ "Lab Members". Bardwell Lab. Retrieved 3 August 2016.
- ^ Koutmos, Markos; Datta, Supratim; Pattridge, Katherine A.; Smith, Janet L.; Matthews, Rowena G. (2009-11-03). "Insights into the reactivation of cobalamin-dependent methionine synthase". Proceedings of the National Academy of Sciences of the United States of America. 106 (44): 18527–18532. Bibcode:2009PNAS..10618527K. doi:10.1073/pnas.0906132106. ISSN 1091-6490. PMC 2765455. PMID 19846791.
- ^ Hondorp, Elise R.; Matthews, Rowena G. (May 2009). "Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli". Journal of Bacteriology. 191 (10): 3407–3410. doi:10.1128/JB.01722-08. ISSN 1098-5530. PMC 2687158. PMID 19286805.
- ^ Yamada, K.; Chen, Z.; Rozen, R.; Matthews, R. G. (2001-12-11). "Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase". Proceedings of the National Academy of Sciences. 98 (26): 14853–14858. Bibcode:2001PNAS...9814853Y. doi:10.1073/pnas.261469998. ISSN 0027-8424. PMC 64948. PMID 11742092.
- ^ Jump up to: a b Guenther, Brian D.; Sheppard, Christal A.; Tran, Pamela; Rozen, Rima; Matthews, Rowena G.; Ludwig, Martha L. (April 1999). "The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia". Nature Structural Biology. 6 (4): 359–365. doi:10.1038/7594. ISSN 1545-9985. PMID 10201405. S2CID 23529857.
- ^ "Active Emeritus". Biological Chemistry. 2014-08-13. Retrieved 2019-09-26.
- ^ Multiple sources:
- Drennan, C. L.; Matthews, R. G.; Ludwig, M. L. (December 1994). "Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes". Current Opinion in Structural Biology. 4 (6): 919–929. doi:10.1016/0959-440X(94)90275-5. hdl:2027.42/31943. ISSN 0959-440X. PMID 7712296.
- Ludwig, Martha L.; Matthews, Rowena G. (1997). "Structure-Based Perspectives on B12-Dependent Enzymes". Annual Review of Biochemistry. 66 (1): 269–313. doi:10.1146/annurev.biochem.66.1.269. PMID 9242908.
- 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". Nat. Struct. Mol. Biol. 6: 359–365. doi:10.2210/pdb1b5t/pdb.
- ^ Matthews, Rowena G. (2009-09-25). "A love affair with vitamins". The Journal of Biological Chemistry. 284 (39): 26217–26228. doi:10.1074/jbc.X109.041178. ISSN 1083-351X. PMC 2785309. PMID 19596855.
- ^ Matthews, R. G. (2009). "Cobalamin- and corrinoid-dependent enzymes". Metal Ions in Life Sciences. 6: 53–114. doi:10.1515/9783110436587-006. ISBN 978-3-11-044279-3. PMC 3120101. PMID 20877792.
- ^ Matthews, Rowena G.; Koutmos, Markos; Datta, Supratim (December 2008). "Cobalamin-dependent and cobamide-dependent methyltransferases". Current Opinion in Structural Biology. 18 (6): 658–666. doi:10.1016/j.sbi.2008.11.005. ISSN 1879-033X. PMC 2639622. PMID 19059104.
- ^ Beinert, Helmut; Stumpf, Paul K.; Wakil, Salih J. (2004). "David Ezra Green". Biographical Memoirs. 84. National Academies Press: 112–44. PMID 15484418.
External links[edit]
- National Academy of Sciences InterViews podcast with Rowena Matthews
- University of Michigan faculty
- American people of German-Jewish descent
- American people of Russian-Jewish descent
- American women biochemists
- Living people
- Members of the United States National Academy of Sciences
- University of Michigan alumni
- Radcliffe College alumni
- Members of the American Philosophical Society
- Members of the National Academy of Medicine
- Fellows of the American Academy of Arts and Sciences
- American women academics
- 21st-century American women
- 1938 births