Rowena Green Matthews Explained

Rowena Green Matthews
Birth Place:Cambridge, England
Fields:Biochemistry
Workplaces:University of Michigan
Alma Mater:University of Michigan
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Doctoral Advisor:Vincent Massey
Known For:Studies of cobalamin and folic acid
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Birth Name:Rowena Green

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.

Early life and education

Matthews was born in Cambridge, England while her father, biochemist David E. Green, was on sabbatical there.[3] 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

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.[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.

Awards

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), 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.

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. 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

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.[22]

Selected publications

Personal life

Matthews is the eldest daughter of biochemist David E. Green and the aunt of United States Senator Tammy Baldwin.[26]

External links

Notes and References

  1. Web site: Rowena Green Matthews from Ann Arbor, Michigan VoterRecords.com. voterrecords.com. 2019-09-26.
  2. Web site: Rowena Matthews, Ph.D.. University of Michigan, Ann Arbor. 3 August 2016. 2014-08-13.
  3. Book: Shane. Barry. Milstein. Sheldon. Kapatos. Gregory. Levine. Robert A.. Shane. Barry. 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. 2002. Springer US. Boston, MA. 9781461509455.
  4. Web site: Tangs for the memories Michigan Today. michigantoday.umich.edu. 20 September 2017. 2019-09-26.
  5. Matthews. Rowena G. . Ruth Hubbard . Paul K. Brown . George Wald. Tautomeric forms of metarhodopsin. Journal of General Physiology. 1963. 47. 2 . 215–240. 10.1085/jgp.47.2.215 . 14080814 . 2195338.
  6. Web site: Rowena Matthews. University of Michigan Faculty History Project. 3 August 2016.
  7. Web site: Memoir Faculty History Project. www.lib.umich.edu. 2019-09-26.
  8. Web site: Emeritus Faculty. 2018-03-23. Life Sciences Institute. 2019-09-26.
  9. News: Repligen Corporation Award in Chemistry of Biological Processes. The Repligen Award.
  10. Web site: Matthews. Rowena. Rowena Matthews-National Academy of Sciences.
  11. Web site: Matthews. Rowena. Directory: IOM Member-Rowena G. Matthews, Ph.D.. Global directory. dead. https://archive.today/20130815063247/http://www.iom.edu/global/directory/detail.aspx?id=0000060661. 2013-08-15.
  12. Web site: American Philosophical Society Honors HHMI Scientists and Board Members. HHMI News. 7 August 2016. 7 May 2009.
  13. Web site: Dr. Rowena G. Matthews. American Philosophical Society Member History. 7 August 2016.
  14. Web site: Medical Advisory Board. Howard Hughes Medical Institute. 25 March 2015.
  15. Web site: Leadership and Governance. National Academy of Sciences. 25 March 2015.
  16. Web site: Lab Members. Bardwell Lab. 3 August 2016.
  17. 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. 10.1073/pnas.0906132106. 1091-6490. 2765455. 19846791. 2009PNAS..10618527K. free.
  18. 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. 10.1128/JB.01722-08. 1098-5530. 2687158. 19286805.
  19. 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. 10.1073/pnas.261469998. 11742092. 64948. 0027-8424. 2001PNAS...9814853Y. free.
  20. 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. 10.1038/7594. 10201405. 23529857. 1545-9985.
  21. Web site: Active Emeritus. 2014-08-13. Biological Chemistry. 2019-09-26.
  22. 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. 0959-440X. 7712296. 10.1016/0959-440X(94)90275-5. 2027.42/31943. free.
    • Ludwig. Martha L.. Matthews. Rowena G.. 1997. Structure-Based Perspectives on B12-Dependent Enzymes. Annual Review of Biochemistry. 66. 1. 269–313. 10.1146/annurev.biochem.66.1.269. 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. 10.2210/pdb1b5t/pdb.
  23. Matthews. Rowena G.. 2009-09-25. A love affair with vitamins. The Journal of Biological Chemistry. 284. 39. 26217–26228. 10.1074/jbc.X109.041178. 1083-351X. 2785309. 19596855. free.
  24. 20877792. 3120101. 2009. Matthews. R. G.. Cobalamin- and corrinoid-dependent enzymes. Metal Ions in Life Sciences. 6. 53–114. 10.1515/9783110436587-006. 978-3-11-044279-3 .
  25. Matthews. Rowena G.. Koutmos. Markos. Datta. Supratim. December 2008. Cobalamin-dependent and cobamide-dependent methyltransferases. Current Opinion in Structural Biology. 18. 6. 658–666. 10.1016/j.sbi.2008.11.005. 1879-033X. 2639622. 19059104.
  26. Beinert. Helmut. Stumpf. Paul K.. Wakil. Salih J.. David Ezra Green. Biographical Memoirs. 2004. 84. 112–44. National Academies Press. 15484418.

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