Curriculum Vitae

Personal Data

Rowena Green Matthews

Research Professor, Life Sciences Institute

G. Robert Greenberg Distinguished University Professor of Biological Chemistry

Research Professor, Biophysics Research Division
Professor, Department of Chemistry

4002 Life Sciences Institute
210 Washtenaw Ave.
Ann Arbor, MI 48109-2216
Tel: (734) 764-9459
Fax: (734) 763-6492
E-mail: rmatthew - at - umich.edu
Website

Education

B.A. Biology (Summa Cum Laude), Radcliffe College, Cambridge, MA, 1960
Ph.D. Biophysics, University of Michigan, Ann Arbor, MI, 1969
Research Director: Dr. Vincent Massey

Postdoctoral training

Postdoctoral Scholar, Mentor : Charles H. Williams, Jr.
The University of Michigan, Ann Arbor, MI, 1971-74

Academic Appointments

Research Assistant
Laboratory of Professor George Wald
Department of Biology
Harvard University, Cambridge, MA
1960-1963

Instructor
Department of Biology
University of South Carolina, Columbia, SC
1964-1965

Research Investigator
Department of Biological Chemistry
University of Michigan, Ann Arbor, MI
1974-1975

Research Chemist
Veterans Administration Hospital
Ann Arbor, MI
1975-1978

Assistant Professor
Department of Biological Chemistry
University of Michigan, Ann Arbor, MI
1978-1981

Assistant Research Biophysicist
Biophysics Research Division
University of Michigan, Ann Arbor, MI
1978-1981

Associate Professor
Department of Biological Chemistry
University of Michigan, Ann Arbor, MI
1981-1986

Associate Research Biophysicist
Biophysics Research Division
University of Michigan, Ann Arbor, MI
1981-1986

Professor
Department of Biological Chemistry
University of Michigan, Ann Arbor, MI
1986-present

Research Scientist
Biophysics Research Division
University of Michigan, Ann Arbor, MI
1986-1997

Associate Chair
Biological Chemistry
University of Michigan, Ann Arbor, MI
1988-1993

The G. Robert Greenberg Distinguished University Professor
Department of Biological Chemistry
University of Michigan, Ann Arbor, MI
1995-present

Chair
Biophysics Research Division
University of Michigan, Ann Arbor, MI
1996-2001

Senior Research Scientist
Biophysics Research Division
University of Michigan, Ann Arbor, MI
1997-present

Senior Research Professor and Charter Faculty Member
Life Sciences Institute
University of Michigan, Ann Arbor, MI
2002-present

Honors and Awards

Bibliography (abstracts not included)

Publications in Scholarly Journals

1. Matthews, R.G., Hubbard, R., Brown, P.K., and Wald, G. Tautomeric forms of metarhodopsin. J. Gen. Physiol. 47, 215-240 (1963)
2. Matthews, R.G., and Massey, V. The isolation of old yellow enzyme in free and complexed forms. J. Biol. Chem. 244, 1779-1786 (1969)
3. Massey, V., Muller, F., Feldberg, R., Schuman, M., Sullivan, P.A., Howell, L.G., Mayhew, S.G., Matthews, R.G., and Foust, G.P. The reactivity of flavoproteins with sulfite. J. Biol. Chem. 244, 3999-4006 (1969)
4. Massey, V., Strickland, S., Mayhew, S.G., Howell, L.G., Engel, P.C., Matthews, R.G., Schuman, M., and Sullivan, P.A. The production of super-oxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen. Biochem. Biophys. Res. Comm. 36, 891-897 (1969)
5. Matthews, R.G., Arscott, L.D., and Williams, C.H., Jr. Isolation, characterization, and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase. Biochim. Biophys. Acta 370, 26-38 (1974)
6. Matthews, R.G., and Williams, C.H., Jr. Identification of the thiol residues involved in modification of pig heart lipoamide dehydrogenase by cupric ion and by iodoacetamide. Biochim. Biophys. Acta 370, 39-48 (1974)
7. Matthews, R.G., Massey, V., Sweeley, C.C. The identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. J. Biol. Chem. 250, 9294-9298 (1975)
8. Matthews, R.G., and Williams, C.H., Jr. Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. J. Biol. Chem. 251, 3956-3964 (1976)
9. Matthews, R.G., Ballou, D.P., Thorpe, C., and Williams, C.H. Ion pair formation as a rationalization of the pH profiles for the reactivity of oxidized pig heart lipoamide dehydrogenase with dihydrolipoamide and two-electron reduced enzyme with lipoamide and iodoacetamide. J. Biol. Chem. 252, 3199-3207 (1977)
10. Thorpe, C., Matthews, R.G., and Williams, C.H., Jr. Acyl-CoA dehydrogenase from pig kidney: purification and properties. Biochemistry 18, 331-337 (1979)
11. Williams, C.H., Jr., Arscott, L.D., Matthews, R.G., Thorpe, C., and Wilkinson, K.D. Methodology employed for anaerobic spectrophotometric titrations and for computer assisted analysis of the data. Methods in Enzymology 62D, pp. 185-198 (1979)
12. Matthews, R.C., Ballou, D.P., and Williams, C.H., Jr. Reactions of pig heart lipoamide dehydrogenase with pyridine nucleotides: evidence for an effector role for bound oxidized pyridine nucleotide. J. Biol. Chem. 254, 4974-4981 (1979)
13. Matthews, R.G., and Haywood, B.J. Inhibition of pig liver methylenetetrahydrofolate reductase by dihydrofolate: some mechanistic and regulatory implications. Biochemistry 18, 4845-4851 (1979)
14. Matthews, R.G., and Baugh, C.M. Interactions of pig liver methylenetetrahydrofolate reductase with methylenetetrahydropteroylpolyglutamate substrates and with dihydropteroylpolyglutamate inhibitors. Biochemistry 19, 2040-2045 (1980)
15. Matthews, R.G., and Kaufman, S. Characterization of the dihydropterin reductase activity of pig liver methylenetetrahydrofolate reductase. J. Biol. Chem. 255, 6014-6017 (1980)
16. Matthews, R.G. Are the redox properties of tetrahydrofolate cofactors utilized in folate-dependent reactions? Fed. Proc. 41, 2600-2604 (1982)
17. Daubner, S.C., and Matthews, R.G. Purification and Properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem. 257, 140-145 (1982)
18. Matthews, R.G., Ross, J., Baugh, C.M., Cook, J.D., and Davis, L. Interactions of pig liver serine hydroxymethyltransferase with methyltetrahydropteroylpolyglutamate inhibitors and with tetrahydropteroylpolyglutamate substrates. Biochemistry 21, 1230-1238 (1982)
19. Matthews, R.G. Studies on the methylene/methyl interconversion catalyzed by methylenetetrahydrofolate reductase from pig liver. Biochemistry 21, 4165-4171 (1982)
20. Matthews, R.G., and Daubner, S.C. (1982) Modulations of methylenetetrahydrofolate reductase activity by S-adenosylmethionine and by dihydrofolate and its polyglutamate analogues, in Advances in Enzyme Regulation 20, 123-131
21. Vanoni, M.A., Ballou, D.P., and Matthews, R.G. Methylenetetrahydrofolate reductase: Steady-state and Rapid Reaction Studies on the NADPH- methylenetetrahydrofolate, NADPH-menadione and Methyltetrahydrofolate- menadione Oxidoreductase Activities of the Enzyme. J. Biol. Chem. 258, 11510-11514 (1983)
22. Ross, J., Green, J., Baugh, C.M., MacKenzie, R.E., and Matthews, R.G. Studies on the polyglutamate specificity of methylenetetrahydrofolate dehydrogenase from pig liver. Biochemistry 23, 1796-1801 (1984)
23. Vanoni, M.A., and Matthews, R.G. Kinetic isotope effects on the oxidation of NADPH by the flavoprotein methylenetetrahydrofolate reductase. Biochemistry 23, 5272-5279 (1984)
24. Lu, Y.-Z., Aiello, P.D., and Matthews, R.G. Studies on the polyglutamate specificity of thymidylate synthase from fetal pig liver. Biochemistry 23, 6870-6876 (1984)
25. Matthews, R.G., Vanoni, M.A., Hainfeld, J.F., and Wall, J. Methylenetetrahydrofolate reductase: evidence for spatially distinct subunit domains obtained by scanning transmission electron microscopy and limited proteolysis. J. Biol. Chem. 259 11647-11650 (1984)
26. Klinman, J.P., and Matthews, R.G. Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions. J. Am. Chem. Soc. 107, 1058-1060 (1985)
27. Zydowsky, T.M., Courtney, L.F., Frasca, V., Kobayashi, K., Shimuzu, M., Yuen, L.-O., Matthews, R.G., Benkovic, S.J., and Floss, H.G. Stereochemical analysis of methyl transfer catalyzed by cobalamin-dependent methionine synthase from E. coli B. J. Am. Chem. Soc. 108, 3152-3153 (1986)
28. Sumner, J., Jencks, D.A., Khani, S., and Matthews, R.G. Photoaffinity labeling of methylenetetrahydrofolate reductase with 8-azido-S-adenosylmethionine. J. Biol. Chem. 261, 7697-7700 (1986)
29. Frasca, V., Riazzi, B.S., and Matthews, R.G. (1986) In vitro Inactivation of Methionine Synthase by Nitrous Oxide. J. Biol. Chem. 261, 15823-15826
30. Matthews, R.G. (1986) Preparation and Analysis of Pteroylpolyglutamate Substrates and Inhibitors. Methods Enzymol. 122, pp. 333-339
31. Matthews, R.G. (1986) Methylenetetrahydrofolate Reductase from Pig Liver. Methods Enzymol. 122, 372-381
32. Jencks, D.A., and Matthews, R.G. (1987) Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine: Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium, J. Biol. Chem. 262, 2485-2493
33. Matthews, R.G., Ghose, C., Green, J.M., Matthews, K. D., and Dunlap, R.B. (1987) Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes. Adv. Enzyme Regulation 26, 157-171
34. Green, J.M., Ballou, D.P., and Matthews, R.G. (1988) Examination of the role of methylenetetrahydrofolate reductase in incorporation of methyltetrahydrofolate into cellular metabolism. FASEB Journal 2, 42-47.
35. Matthews, R.G., and Neidhardt, F.C. (1988) Abnormal induction of heat shock proteins in Escherichia coli mutant strain with a deficiency in adenosylmethionine synthetase activity. J. Bacteriol. 170, 1582-1588.
36. Green, J.M., MacKenzie, R.E., and Matthews, R.G. (1988) Substrate flux through methylenetetrahydrofolate dehydrogenase: Predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration. Biochemistry 27, 8014-8022.
37. Frasca, V., Banerjee, R.V., Dunham, W.R., Sands, R.M., and Matthews, R.G. (1988) Cohalamin-dependent methionine synthase from Escherichia coli B: Election paramagnetic resonance spectra of the inactive form and the active methylated form of the enzyme. Biochemistry 27, 8458-8465.
38. Matthews, R.G., and Neidhardt, F.C. (1989) Elevated serine catabolism is associated with the heat shock response in Escherichia coli. J. Bacteriol. 171, 2619-2625.
39. Banerjee, R.V., Johnston, N.L., Sobeski, J.K., Datta, P., and Matthews, R.G. (1989) Cloning and sequence analysis of the Escherichia coli met H gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264, 13888-13895.
40. Banerjee, R.V., Harder, S.F., Ragsdale, S.W., and Matthews, R.G. (1990) Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study. Biochemistry 29, 1129-1133.
41. Matthews, R.G., and Banerjee, R.V. (1990) Cobalamin-dependent methionine synthase. FASEB Journal, 4, 1450-1459.
42. Banerjee, R.V., Ragsdale, S.W., and Matthews, R.G. (1990) Cobamide-dependentmethyltransferases. Biofactors 2, 147-152.
43. Vanoni, M.A., Lee, S., Floss, H.G., and Matthews, R.G. (1990) The stereochemistry of reduction of methylenetetrahydrofolate to methyltetrahydrofolate reductase, J. Am. Chem. Soc., 3987-3992.
44. Matthews, R.G., and Drummond, J.T. (1990) Providing one carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrotolate reductase and methyltetrahydrofolate-homocysteine methyltransferase. Chem. Rev. 90, 1275-1290.
45. Banerjee, R. V., Frasca, V., Ballou, D. P., and Matthews, R. G. (1990) Participation of cob(I)alamin in the reaction catalyzed by methionine synthase from Escherichia coli: A steady-state and rapid reaction kinetic analysis. Biochemistry 29, 11101-11109.
46. Rohlman, C.E., and Matthews, R.G. (1990) The role of purine biosynthetic intermediates in response to folate stress in Escherichia coli. J.Bacteriol. 172, 7200-7210.
47. Osborne, C., Chen, L.-M., and Matthews, R. G. (1991) Isolation, cloning, mapping and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli. J. Bacteriol. 173, 1729-1737.
48. Ernsting, B. R., Atkinson, M., Ninfa, A., and Matthews, R. G. (1992) Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli. J. Bacteriol. 174, 1109-1118.
49. Lin, R., Ernsting, B., Hirshfield, I. N., Matthews, R. G., Neidhardt, F. C., Clark, R. L., and Newman, E. G. (1992) The lrp gene product regulates expression of lysU in E. coli K-12. J. Bacteriol. 174, 2779-2784.
50. Luschinsky, C. L., Drummond, J. T., Matthews, R. G., and Ludwig, M. (1992) Crystallization and preliminary x-ray diffraction studies on the cobalamin binding domain of methionine synthase from Escherichia coli. J. Mol. Biol. 225, 557-560.
51. González, J., Banerjee, R. V., and Matthews, R. G. (1992) Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: Two solutions to the same chemical problem. Biochemistry 31, 6045-6056.
52. Sumner, J. S., and Matthews, R. G. (1992) Stereochemistry and mechanism of hydrogen transfer between NADPH and methylenetetrahydrofolate in the reaction catalyzed by methylenetetrahydrofolate reductase from pig liver. J. Am. Chem. Soc. 114, 6949-6956.
53. Drummond, J. T., Ogorzalek Loo, R. R., and Matthews, R. G. (l993) Electrospray mass spectrometric analysis of the domains of a large enzyme: Observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase. Biochemistry 32, 9282-9289.
54. Drummond, J. T., Huang, S., Blumenthal, R. M., and Matthews, R. G. (l993) Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli. Biochemistry 32: 9290-9295.
55. Ernsting, B. R., Denninger, J. W., Blumenthal, R. M., and Matthews, R. G. (l993) Regulation of the gltBDF operon of Escherichia coli: how is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein? J. Bacteriol.175, 7160-7169.
56. Bianchi, V., Eliasson, R., Fontecave, M., Mulliez, E., Hoover, D. M., Matthews, R. G., and Reichard, P. (1993) Flavodoxin is required for the activation of anaerobic ribonucleotide reductase. Biochem. Biophys. Res. Commun. 197, 792-797.
57. Drummond, J. T., and Matthews, R. G. (l994) Nitrous oxide degradation by cobalamin-dependent methionine synthase: Characterization of the reactants and products in the inactivation reaction. Biochemistry 33, 3732-3741.
58. Drummond, J. T., and Matthews, R. G. (l994) Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli: Characterization of the damage to the enzyme and prosthetic group. Biochemistry 33, 3742-3750.
59. Goyette, P., Sumner, J., Milos, R., Duncan, A. M. V., Rosenblatt, D. S., Matthews, R. G., and Rozen,R. (l994) Isolation and chromosomal assignment of a cDNA for human methylenetetrahydrofolate reductase (MTHFR), with identification of mutations in MTHFR deficiency. Nature Genetics 7, 195-200.
60. Calvo, J. M., and Matthews, R. G. (1994) The leucine-responsive regulatory protein (Lrp), a global regulator of metabolism in Escherichia coli. Microbiological Reviews 58, 466-490.
61. Drennan, C. L., Huang, S., Drummond, J. T., Matthews, R. G., and Ludwig, M. L. (l994) How a protein binds B12: A 3.0 Å structure of the B12-binding domains of methionine synthase. Science 266, 1669-1674.
62. Drennan, C. L., Matthews, R. G., and Ludwig, M. L. (l994) Cobalamin-dependent methionine synthase: The structure of a methylcobalamin-binding fragment and its implications for other B12-dependent enzymes. Current Opinions in Structural Biology 4, 919-929.
63. Ferrario, M., Ernsting, B. R., Wiese, D., Borst, D., Blumenthal, R. M., and Matthews, R. G. (l995) The leucine-responsive regulatory protein of Escherichia coli negatively regulates transcription of ompC and micF and positively regulates translation of ompF. J. Bacteriol. 177, 103-113.
64. Eichel, J., González, J. C., Hotze, M., Matthews, R. G., and Schröder, J. (1995) Vitamin B12-independent L-methionine synthase from a higher plant (Canthaanthus roseus): Molecular characterization, heterologous expression, and enzyme properties. Eur. J. Biochem. 230, 1053-1058.
65. Webb, H. K., and Matthews, R. G. (l995) 4-Chlorothreonine is both a substrate for and an inhibitor of serine hydroxymethyltransferase. J. Biol. Chem. 270, 17204-17209.
    
66. Drummond, J. T., Jarrett, J., González, J. C., Huang, S., and Matthews, R. G. (l995) Characterization of non-radioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes. Anal. Biochem. 228, 323-329.
67. 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., van den Heuvel, L. P., and Rozen, R. (1995) A candidate genetic risk factor for vascular disease: A common mutation at the methylenetetrahydrofolate reductase locus. Nature Genetics 10, 111-113.
68. Lipman, R. S. A., Bailey, S. W., Jarrett, J. T., Matthews, R. G., and Jorns, M. S. (l995) Stereospecificity of folate binding to DNA photolyase from Escherichia coli. Biochemistry 34, 11217-11220.
69. Drennan, C. L., Matthews, R. G., Rosenblatt, D. S., Ledley, F. D., Fenton, W. A., and Ludwig, M. L. (l996) Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Proc. Natl. Acad. Sci. 93, 5550-5555.
70. Amaratunga, M., Fluhr, K., Jarrett, J. T., Drennan, C. L., Ludwig, M. L., Matthews, R. G., and Scholten, J. D. (l996) A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of E. coli methionine synthase: Initial characterization of the seven mutant proteins. Biochemistry 35, 2453-2463.
71. Jarrett, J. T., Amaratunga, M., Drennan, C. L., Scholten, J. D., Sands, R. H., Ludwig, M. L., and Matthews, R. G. (l996) Mutations in the B12-binding region of methionine synthase: How the protein controls methylcobalamin reactivity. Biochemistry 35, 2464-2475.
72. Jarrett, J. T., Drennan, C. L., Amaratunga, M., Scholten, J. D., Ludwig, M. L., and Matthews, R. G. (l996) A protein radical cage slows photolysis of methylcobalamin in methionine synthase from Escherichia coli. Bioorganic and Medicinal Chemistry, 4, 1237-1246.
73. Ludwig, M. L., Drennan, C. L., and Matthews, R. G. (l996) The reactivity of B12-Cofactors: The proteins make a difference. Structure 4, 505-512.
74. González, J. C., Peariso, K., Penner-Hahn, J. E., and Matthews, R. G. (l996) Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme. Biochemistry 35, 12228-12234.
75. Dixon, M. M., Huang, S., Matthews, R. G., and Ludwig, M. L. (l996) The structure of the C-terminal domain of methioine synthase: presenting S-adenosylmethionne for reductive methylation of B12. Structure 4, 1263-1275.
76. Borst, D. W., Blumenthal, R. M., and Matthews, R. G. (l996) Use of an in vivo titration method to study a global regulator: the effect of varying Lrp levels on the expression of gltBDF in Escherichia coli. J. Bacteriol. 178, 6904-6912.
77. Jarrett, J. T., Goulding, C., Fluhr, K., Huang, S., and Matthews, R. G. (l997) Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli. Methods in Enzymology 281, 196-213.
78. Hoover, D. M., Jarrett, J. T., Sands, R. H., Dunham, W. R., Ludwig, M. L., and Matthews, R. G. (l997) Interaction of E. coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor. Biochemistry 36, 127-138.
79. Ludwig, M. L., and Matthews, R. G. (l997) B12(cobalamin)-dependent enzymes. Annual Review ofBiochemistry 66, 269-313.
80. Wiese, D. E., II, Ernsting, B. R., Blumenthal, R. M., and Matthews, R. G. (l997) A nucleoprotein activation complex between the leucine-responsive regulatory protein and DNA upstream of the gltBDF operon in Escherichia coli. J. Mol. Biol. 270, 139-151.
81. Goulding, C. W., Postigo, D., and Matthews, R. G. (l997) Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry 36, 8082-8091.
82. Matthews, R. G., and Goulding, C. W. (l997) Enzyme-catalyzed methyl tranfers to thiols: the role of zinc. Curr. Opin. Chemical Biology 1, 332-339.
83. Bhagwat, S., Rice, M. R., Matthews, R. G., and Blumenthal, R. M. (l997) Use of an inducible regulatory protein to identify members of a regulon: application to the regulon controlled by the leucine-responsive regulatory protein (Lrp) in Escherichia coli. J. Bacteriol. 179, 6254-6263.
84. Goulding, C. W., and Matthews, R. G. (l997) Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry 36, 15749-15757.
85. Jarrett, J. T., Choi, C. Y., and Matthews, R. G. (l997) Changes in protonation associated with substrate binding and cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry 36, 15739-15748.
86. Jarrett, J. T., Huang, S., and Matthews, R. G. (l998) Methionine synthase exists in two distinct conformations that differ in reactivity towards methyltetrahydrofolate, adenosylmethionine, and flavodoxin. Biochemistry 37, 5372-5382.
87. Walker, L. A., Jarrett, J. T., Anderson, N., Pullen, S., Matthews, R. G., and Sension, R. J. (l998) Time-resolved spectroscopic studies of B12 coenzymes: The identification of a metastable cob(III)alamin photoproduct in the photolysis of methylcobalamin. J. Am. Chem. Soc. 120, 3597-3603.
88. Peariso, K., Goulding, C. W., Huang, S., Matthews, R. G., and Penner-Hahn, J. E. (l998) Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: the role of zinc in the methylation of homocysteine. J. Am. Chem. Soc. 120, 8410-8416.
89. Jarrett, J. T., Hoover, D. M., Ludwig, M. L., and Matthews, R. G. (l998) The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of cob(II)alamin enzyme. Biochemistry 37, 12649-12658.
90. Guenther, B. D., Sheppard, C. A., Tran, P., Rozen, R., Matthews, R. G., and Ludwig, M. L. (l999) The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli: a model for the role of folate in ameliorating hyperhomocysteinemia in humans. Nature Structural Biology, 6, 359-365.
91. Sheppard, C. A., Trimmer, E. E., and Matthews, R. G. (l999) Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase. J. Bacteriol. 181, 718-725.
92. VanBogelen, R. A., Greis, K. D., Blumenthal, R. M., Tani, T. H., and Matthews, R. G. (l999) Mapping regulatory networks in microbial cells. Trends Microbiol. 7, 1540-1546.
93. Zhou, Z. S., Peariso, K., Penner-Hahn, J. E., and Matthews, R. G. (l999) Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Biochemistry, 38, 15915-15926.
94. Matthews, R. G., Cui, Y., Friedberg, D., and Calvo, J. M. (2000) Wild type and Hexahistidine-Tagged Derivatives of the Leucine-Responsive Regulatory Protein from Escherichia coli. Meth. Enzymol. 324, 322-329.
95. Hall, D. A., Jordan-Starck, T. C., Loo, R. O., Ludwig, M. L., and Matthews, R. G. (2000) Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39, 10711-10719.
96. Smith, A. E., and Matthews, R. G. (2000) The protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase. Biochemistry 39, 13880-13890.
97. Zhou, Z. S., Smith, A. E., and Matthews, R. G. (2000) Selenohomocysteine: One-step synthesis from selenomethionine and kinetic analysis as substrate for methionine synthases Bioorganic & Medicinal Chemistry Letters 10, 2471-2475.
98. Peariso, K., Zhou, Z. S., Smith, A. E., Matthews, R. G., and Penner-Hahn, J. E. (2001) Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase: structural changes on homocysteine binding. Biochemistry 40, 987-993.
99. Trimmer, E. E., Ballou, D. P., and Matthews, R. G. (2001) Methylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies. Biochemistry 40, 6205-6215.
100. Trimmer, E. E., Ballou, D. P., Ludwig, M. L., and Matthews, R. G. (2001) Folate activation and catalysis in methylenetetrahydrofolate reudtase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry 40, 6216-6226.
101. Bandarian, V., and Matthews, R. G. (2001) Quantitation of rate enhancements obtained by binding of cobalamin to methionine synthase. Biochemistry 40, 5056-5064.
102. Matthews, R. G. (2001) Cobalamin-dependent methyltransferases. Accounts of Chemical Research 34, 681-689.
103. Paul, L., Blumenthal, R. M., and Matthews, R. G. (2001) Activation from a distance: roles of Lrp and IHF in transcriptional activation of gltBDF. J. Bacteriol. 183, 3910-3918.
104. Hall, D. A., Van der Kooi, C. W., Stasik, C. N. Stevens, S. Y., Zuiderweg, E. R. P., and Matthews, R. G. (2001) Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase. Proc. Natl. Acad. Sci., U. S. A. 98, 9521-9526.
105. Yamada, K., Chen, Z., Rozen, R. and Matthews, R. G. (2001) Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. Proc. Natl. Acad. Sci., USA, 98, 14853-14858.
106. Matthews, R. G. (2002) Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications. The Chemical Record 2, 4-12.
107. Bandarian, V., Pattridge, K. A., Lennon, B. W., Huddler, D. P., Matthews, R. G., and Ludwig, M. L. (2002) Domain alternation in B12-dependent methionine synthase: switching to the activation conformation. Nature Structural Biol. 9, 53-56.
108. Sirovatka, J. M., Matthews, R. G., and Finke, R. G. (2002) Providing a chemical basis towards understanding the histidine base-on motif of methylcobalamin-dependent methionine synthase: an improved purification of methylcobinamide, plus thermodynamic studies of MeCbi+ binding exogenous imidazole and pyridine bases. Inorg. Chem. 41, 6217-6224.
109. Tani, T. H., Khodursky, A., Blumenthal, R. M., Brown, P. O., and Matthews, R. G. (2002) Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proc. Natl. Acad. Sci., USA, 99, 13471-13476.
110. Kacprzak, M., Lewandowska, I., Matthews, R. G., and Paszewski, A. (2003) The Aspergillus nidulans metH gene encoding methionine synthase is regulated by homocysteine and choline, which can be synthesized from betaine. Biochem. J. 376, 517-524.
111. Bandarian, V., Ludwig, M. L., and Matthews, R. G. (2003) Factors modulating conformational equlibria in large modular proteins: a case study with cobalamin-dependent methionine synthase. Proc. Natl. Acad. Sci., U. S. A. 100, 8156-8163.
112. Bandarian V., and Matthews, R. G. (2004) Measurement of energetics of conformational change in cobalamin-dependent methionine synthase. Meth. Enzymol. 380, 152-169.
113. Matthews, R. G., Smith, A. E., Zhou, Z. S., Taurog, R., Bandarian, V., Evans, J. C. and Ludwig, M. L.(2003) Cobalamin-dependent and cobalamin-independent methionine synthases: are there two solutions to the same chemical problem? Helvetica Chimica Acta 86, 3939-3954. [Special issue to celebrate the 75th birthday of Dulio Arigoni]
114. Dorweiler, J. S., Finke, R. G., and Matthews, R. G. (2003) Cobalamin-dependent methionine synthase: probing the role of the axial base in catalysis of methyl transfer between methyltetrahydrofolate and exogenous cob(I)alamin or cob(I)inamide. Biochemistry 42, 14653-14662.
115. Evans, J. C., Huddler, D. P., Hilgers, M. T., Romanchuk, G., Matthews, R. G., and Ludwig, M. L. (2004) Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase. Proc. Natl. Acad. Sci., U. S. A.. 100, 3729-3736.
116. Manning, E. R., and Matthews, R. G. (2004) Oxidative stress inactivates cobalamin-independent methionine synthase in Escherichia coli. PLoS Biology 2, 1738-1756.

Chapters in Books

1. Massey, V., Matthews, R.G., Foust, G.P., Howell, L.G., Williams, C.H., Jr., Zanetti, G., and Ronchi, S. A New Intermediate in TPNH-Linked Flavoproteins in Pyridine Nucleotide-Dependent Dehydrogenases (Sund, H., ed.) pp. 393-411, Springer-Verlag, Berlin (1970)
2. Matthews, R.G., and Massey, V. Free and Complexed Forms of Old Yellow Enzyme in Third International Symposium on Flavins and Flavoproteins (Kamin, H., ed.) pp. 329-348, University Park Press, Baltimore, Maryland (1971)
3. Matthews, R.G., Wilkinson, K.D., Ballou, D.P., and Williams, C.H., Jr. The Role of NAD as a Activator in the NADH-Lipoamide Reductase Reaction of Pig Heart Lipoamide Dehydrogenase in Fifth International Symposium on Flavins and Flavoproteins (Singer, T., ed.), pp. 464-472, Elsevier Scientific Publishing Company, Amsterdam (1976)
4. Thorpe, C., Matthews, R.G., and Williams, C.H., Jr. Purification and Some Properties of Acyl-CoA Dehydrogenase from Pig Kidney in Flavins and Flavoproteins: Proceedings of Sixth International Symposium, Japan Scientific Societies Press, pp. 209-216 (1978)
5. Matthews, R.G., Ballou, D.P., and Williams, C.H., Jr. Studies on Reactions of Lipoamide Dehydrogenase with Pyridine Nucleotides in Flavins and Flavoproteins: Proceedings of Sixth International Symposium. Japan Scientific Societies Press (1978)
6. Matthews, R.G., and Haywood, B.J. Inhibition of Pig Liver Methylene- tetrahydrofolate Reductase by Dihydrofolate in The Chemistry and Biology of Pteridines (Kisliuk, R.L., and Brown, G.M., eds.) Elsevier, North Holland, pp. 459-464 (1979)
7. Daubner, S.C., and Matthews, R.G., Purification and Properties of Methylenetetrahydrofolate Reductase from Pig Liver, in Flavins and Flavoproteins (Massey, V., and Williams, C.H., Jr., eds.) Elsevier - North Holland, New York, pp. 165-172 (1981)
8. Daubner, S.C., Kropf, E., and Matthews, R.G. Interactions of S-adenosyl-methionine with Methylenetetrahydrofolate Reductase, in Transmethylation (Borchardt, R., Creveling, C.R., and Usdin, E., eds.) pp. 617-620, MacMillan (1982)
9. Matthews, R.G., Hubbard, R., Brown, P.K., and Wald, G. Tautomeric Forms of Metarhodopsin in Benchmark Papers in Biochemistry, Vol. 3, Molecular Processes in Vision (Abrahamson, E.W., and Ostrey, S.E., eds.) Hutchinson Ross Rublishing Co., Stroudsberg, P.A. (1982)
10. Matthews, R.G., Ross, J., Baugh, C.M., Cook, J.D., and Davis, L. The Role of Folylpolyglutamates in the Regulation of Folate Metabolism, in "Folyl- and Antifolylpolyglutamates" (Goldman, I.D., Chabner, B., and Bertino, J.R., eds.) Advances in Experimental Biology, Plenum Press, pp. 35-44 (1983)
11. Vanoni, M.A., Daubner, S.C., Ballou, D.P., and Matthews, R.G. Studies on Methylenetetrahydrofolate Reductase from Pig Liver: Catalytic Mechanism and Regulation by Adenosylmethionine, in Chemistry and Biology of Pteridines (J.A. Blair, ed.) De Gruyter, Berlin pp. 235-239 (1983)
12. Matthews, R.G. Methionine Biosynthesis, Chapter 13 in Chemistry and Biology of Folates (R.L. Blakley and S.J. Benkovic, eds.), John Wiley and Sons, New York, pp. 497-553 (1984)
13. Vanoni, M.A., and Matthews, R.G. Methylenetetrahydrofolate Reductase: An Imperfect Enzyme? in Flavins and Flavoproteins (Bray, R.C., Engel, P.C., and Mayhew, S.G., eds.) Walter de Gruyter, Berlin, pp. 497-500 (1984)
14. Matthews, R.G., Vanoni, M.A., Khani, S., Hainfeld, J.F., and Wall, J., Evidence for Two Spatially Distinct Domains on Each Subunit of Methylene-tetrahydrofolate Reductase in Flavins and Flavoproteins (Bray, R.C., Engel, P.C., and Mayhew, S.G., eds.) Walter de Gruyter, Berlin, pp. 217-220 (1984)
15. Matthews, R.G., Lu, Y.-Z., Green, J.M., and MacKenzie, R.E. The Poly-glutamate Specificities of Four Folate-Dependent Enzymes from Pig Liver, in Proceedings of the Second Workshop on Folyl and Antifolyl Polyglutamates (I.D. Goldman, ed.) Praeger Scientific, New York, pp. 63-75 (1985)
16. Matthews, R.G., Jencks, D.A., Frasca, V., and Matthews, K.D. (1986) Methionine Biosynthesis in Pteridines and Folic Acid Derivatives (B.A. Cooper and V.M. Whitehead, eds.) Walter de Gruyter, Berlin, pp. 697-707
17. Frasca, V., Dunham, W.D., Sands, R.M., Riazzi, B.S., and Matthews, R.G. (1986) Studies of Cobalamin-dependent Methionine Synthase from E. coli B in Pteridines and Folic Acid Derivatives (B.A. Cooper and V.M. Whitehead, eds.) Walter de Gruyter, Berlin, pp. 917-919
18. Green, J., Matthews, R.G., and MacKenzie, R.E. (1986) Stereochemistry of Hydride Transfer to NADP+ by Methylenetetrahydrofolate Dehydrogenase from Pig Liver in Pteridines and Folic Acid Derivatives (B.A. Cooper and V.M. Whitehead, eds.) Walter de Gruyter, Berlin, pp. 901-903
19. Jencks, D.A., and Matthews, R.G. (1986) Inhibition of Methylenetetra- hydrofolate Reductase by Adenosylmethionine in Pteridines and Folic Acid Derivatives (B.A. Cooper and V.M. Whitehead, eds.) Walter de Gruyter, Berlin, pp. 921-923
20. Green, J.M., Ballou, D.P., and Matthews, R.G. (1987) Can methylene-tetrahydrofolate reductase be used to evade the methyl trap? in Flavins and Flavoproteins (D.B. McCormick and D.E. Edmondson, eds.) pp. 229-232
21. Matthews, R.G. (1990) Mammalian Methylenetetrahydrofolate Reductase. in Chemistry and Biochemistry of Flavoenzymes, Vol. I (F. Muller, ed.) CRC Press, Boca Raton, pp. 371-387
22. Ghose, C., Oleinich, R., and Matthews, R.G. (1990) Kinetic studies on thymidylate synthase from Lactobacillus casei in Pteridines and Folic Acid Derivatives (H.-Ch. Curtius and S. Ghisla, eds.) De Gruyter, Berlin, pp. 860-865.
23. Banerjee, R.V., and Matthews, R.G. (1990) Studies on cobalamin-dependent methionine synthase from Escherichia coli K-12 in Pteridines and Folic Acid Derivatives (H-Ch. Curtius and S. Ghisla, eds.) De Gruyter, Berlin, pp. 869-872
24. Vanoni, M. A., Lee, S., Floss, H., and Matthews, R. G. (l991) Stereochemistry of reduction of methylenetetrahydrofolate to methyltetrahydrofolate catalyzed by mammalian methylenetetrahydrofolatereductase. In Flavins and Flavoproteins (Curti, B., Ronchi, S., and Zanetti, G., eds.) De Gruyter, Berlin, pp. 815-818.
25. Matthews, R. G. (l991) Km effects associated with site-directed mutations that reduce the velocity of one half reaction of a ping pong mechanism. In Flavins and Flavoproteins (Curti, B., Ronchi, S., and Zanetti, G., eds.) De Gruyter, Berlin, pp. 593-597.
26. Drummond, J.T., and Matthews, R. G. (l993) Cobalamin-dependent and cobalamin-independent methionine synthases in Escherichia coli: Two solutions to the same chemical problem. In Chemistry and Biology of Pteridines and Folates (Ayling, J. E., Nair, M. G., and Baugh, C. M., eds.) Plenum Press, New York, pp. 687-692.
27. Hoover, D. M., Matthews, R. G., and Ludwig, M. L. (1994) Crystallization and X-ray structure of E. coli flavodoxin. Flavins and Flavoproteins 1993, (K. Yagi, ed.), deGruyter, Berlin, 359-362.
28. Drummond, J. T., and Matthews, R. G. (l995) Cobalamin-dependent methionine synthase: Dissection of a large protein into functional and structural domains. Organic Reactivity: Physical and Biological Aspects (B. T. Golden, R. J. Griffin, and H. Maskill, eds.) Royal Society of Chemistry, Cambridge, pp. 58-72.
29. Matthews, R. G., Green, J. M., and Nichols, B. P. (1996) Folate biosynthesis and the interconversion of folate derivatives. Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd Edition, (F. C. Neidhardt, R. Curtiss, III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. Brooks Low, Jr., B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger, eds.) American Society for Microbiology, Washington, 665-673.
30. Matthews, R. G. (l996) One carbon metabolism. Chapter 36 Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, 2nd Edition, (F. C. Neidhardt, R. Curtiss, III, C. A. Gross, J. L. Ingraham, E. C. C. Lin, K. Brooks Low, Jr., B. Magasanik, W. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger, eds.) American Society for Microbiology, Washington, 600-611.
31. Blumenthal, R. M., Borst, D. W., and Matthews, R. G. (l996) Experimental analysis of global gene regulation in Escherichia coli. Progress in Nucleic Acid Research and Molecular Biology, (Cohn, W. E., and Moldave, K., eds) Volume 55, pp. 1-86, Academic Press, San Diego.
32. Matthews, R. G., Sheppard, C. A., Sumner, J. S., Goyette, P., Frosst, P., and Rozen, R. (l997) Methylenetetrahydrofolate reductase: Comparison of the enzyme from mammalian and bacterialsources. Proceedings of the International Conference on Homocysteine Metabolism: From Basic Science to Clinical Medicine (I. H. Rosenberg, I. Graham, P. Ueland, and H. Refsum, eds.) Kluwer Press, Boston, 37-42.
33. Drennan, C. L., Dixon, M. M., Hoover, D. M., Ludwig, M. L., Jarrett, J. T., Goulding, C. W., and Matthews, R. G. (l998) Cobalamin-dependent methionine synthase from E. coli: Structure and reactivity. in Vitamin B12 and B12 Proteins (Kräutler, B., Arigoni, D., and Golding, B. T. eds.) Wiley-VCH, Weinheim, 133-155.
34. Matthews, R. G., Drummond, J. T., and Webb, H. (l998) Cobalamin-dependent methionine synthase and serine hydroxymethyltransferasee: targets for chemotherapeutic intervention? Adv. Enzyme Regul. 38, 377-392.
35. Matthews, R. G., Sheppard, C., and Goulding, C. (l998) Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology. Eur. J. Biochem. 157:S54-S59.
36. Matthews, R. G. (l999) Methionine synthase. In Chemistry and Biochemistry of B12: Part II: Biochemistry of B12 (R. J. Banerjee, ed.), John Wiley & Sons, New York.
37. Matthews, R. G. (1999) Bi bi ping pong: is there really such a mechanism? In “Enzymatic Mechanisms, P. A. Frey and D. B. Northrop, eds., IOS Press, Amsterdam, pp 155-161.
38. Matthews, R. G. and Ludwig, M. L. (2001) Microbial modeling of human disease: homocysteine metabolism. In Homocysteine in health and disease (R. Carmel and D. W. Jacobsen, eds.), Cambridge University Press, New York, pp. 100-112.
39. Matthews, R. G. (2002) Methylenetetrahydrofolate reductase. In The Encyclopedia of Molecular Medicine (T. Creighton, ed.) Wiley, New York, pp. 2072-2073.
40. Matthews, R. G. (2002) Cobalamin-dependent methionine synthase. In The Encyclopedia of Molecular Medicine (T. Creighton, ed.) Wiley, New York, pp. 2063-2066.
41. Ludwig, M. L., and Matthews, R. G. (2002) B12-dependent methionine synthase: a structure that adapts to catalyze multiple methyl transfer reactions. In Structures and mechanisms: from ashes to enzymes (G. R. Eaton, D. C. Wiley and O. jardetzky, eds.) ACS Symposium Series 827, ACS Washington DC, 186-201.
42. Matthews, R. G. (2002) Making methionine: a love affair with folate. In “Chemistry and Biology of Pteridine and Folates”, S. Milstien, G. Kapatos, R. A. Levine and B. Shane, eds., Kluwer Academic Publishers, Boston, pp. 1-8.
43. Yamada, K., and Matthews, R. G. (2004) Biochemical characterization of human methylenetetrahydrofolate reductase and its polymorpisms. In Human methylenetetrahydrofolate reductase and its polymorphisms (P. Ueland and R. Rozen, eds.) Landes Press, Georgetown, Texas, in press.
44. Bandarian, V., and Matthews, R. G. (2004) B12-containing enzymes. Encyclopedia of Biological Chemistry, Elsevier-Academic Press, San Diego, in press.

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