(to receive a copy of any of these publications, please send an email to
  1. "Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism", Soldano A, Klinke S, Otero LH, Rivera M, Catalano-Dupuy DL, Ceccarelli EA, 2017, PLoS ONE 12(8): e0182535.
  2. "Inhibiting the BfrB:Bfd Interaction in Pseudomonas aeruginosa Causes Irreversible Iron Accumulation in Bacterioferritin and Iron Deficiency in the Bacterial Cytosol", Kate Eshelman*, Huili Yao*, Achala N. D. Punchi Hewage, Jacqueline J. Deay, Josephine R. Chandler, and Mario Rivera, Metallomics, 2017, 9(6), 646-659. (* these authors have equal contribution)
  3. "Bacterioferritin: Structure, Dynamics, and Protein−Protein Interactions at Play in Iron Storage and Mobilization", Mario Rivera, Accounts of Chemical Research, 2017, 50, 331-340.
  4. "Protein-protein Interactions Regulate the Release of Iron Stored in Bacterioferritin", Huili Yao, Yan Wang, and Mario Rivera, Chapter in book: Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria, pp.1109-1117, 2016.
  5. "Protein Dynamics and Ion Traffic in Bacterioferritin Function: A Molecular Dynamics Simulation Study on wild-type and Mutant Pseudomonas Aeruginosa BfrB", Huan Rui, Mario Rivera, and Wonpil Im, Chapter in book: Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria, pp.1118-1129, 2016.
  6. "Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein", Ritesh Kumar, Yifei Qi, Hirotoshi Matsumura, Scott Lovell, Huili Yao, Kevin P. Battaile, Wonpil Im, Pierre Moenne-Loccoz, and Mario Rivera, Biochemistry 2016, 55, 2622-2631.
  7. "Characterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein–Protein Interaction in Solution and Determination of Binding Energy Hot Spots", Yan Wang, Huili Yao, Yuan Cheng, Scott Lovell, Kevin P. Battaile, C. Russell Midaugh, and Mario Rivera, Biochemistry 2015, 54, 6062-6175.
  8. "Antibiotic Activity of Iron-Sequestering Polymers", Nashwa El-Gendy, Jian Qian, Kate Eshelman, Mario Rivera, and Cory Berkland, BioMacromolecules 2015, DOI: 10.1021/bm5016392.
  9. "Concerted Motions Networking Pores and Distant Ferroxidase Centers Enable Bacterioferritin Function and Iron Traffic", Huili Yao; Huan Rui; Ritesh Kumar; Kate Eshelman; Scott Lovell, Kevin P. Battaile; Wonpil Im; and Mario Rivera, Biochemistry 2015, 54, 1611-1627.
  10. "Heme-Iron Utilization by Leptospira interrogans Requires a Heme Oxygenase and a Plastidic-Type Ferredoxin-NADP(+) Reductase", Anabel Soldano; Huili Yao; Mario Rivera; Eduardo A. Ceccarelli; Daniela L. Catalano-Dupuy, Biochimica et biophysica acta, 2014, 1840, 3208-3217.
  11. "Replacing the Axial Ligand Tyrosine 75 or its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa", Ritesh Kumar , Hirotoshi Matsumura , Scott W. Lovell , Huili Yao , Juan Carlos Rodriguez , Kevin P. Battaile , Pierre Moenne-Loccoz , and Mario Rivera, Biochemistry, 2014, 53, 2112-2125.
  12. "Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins", Anatoly M. Ruvinsky, Ilya A. Vakser and Mario Rivera,  Chem. Phys. 2014,140, 115104.
  13. "Bacterioferritin: Structure Function and Protein–Protein Interactions", Mario Rivera, Handbook of Porphyrin Science, Vol. 30, p136-179, 2014.
  14. "The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change", Kumar, R., Slovell, S., Matsumura, H., Battaile, K.,  Moënne-Loccoz, P., and Rivera, M., Biochemistry, 2013, 52 (16), 2705–2707
  15. "Heme Uptake and Metabolism in Bacteria", Benson, D.R., and Rivera, M., Met. Ions Life Sci., 2013, 12, 279-332.
  16. "Protein Dynamics and Ion Traffic in Bacterioferritin", Rui H, Rivera, M, Im W., Biochemistry, 2012, 51, 9900−9910.
  17. "Efficient and selective isotopic labeling of hemes to facilitate the study of multiheme proteins", Fonseca, B.M., Tien, M., Rivera, M., Shi, L., and Louro, R.O. Biotechniques. 2012 April, 1-7, DOI: 10.2144/000113859.
  18. "The Structure of the BfrB-Bfd Complex Reveals Protein-Protein Interactions Enabling Iron Release from Bacterioferritin", Yao H., Wang Y., Lovell S., Kumar R., Ruvinsky A.M., Battaile K.P., Vakser I.A., Rivera M., J Am Chem Soc. 2012 Aug 1. PMID: 22812654.
  19. "Accommodating a Nonconservative Internal Mutation by Water-Mediated Hydrogen Bonding between β-Sheet Strands: A Comparison of Human and Rat Type B (Mitochondrial) Cytochrome b5", Parthasarathy, S., Altuve, A., Terzyan, S., Zhang, X., Kuczera, K., Rivera, M., Benson, D., Biochemistry, 2011, 50 (24), pp 5544–5554.
  20. "Two Distinct Ferritin-like Molecules in Pseudomonas aeruginosa: The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)", Yao, H., Jepkorir, G., Lovell, S., Nama, P., Weeratunga, S., Battaile, K., Rivera, M., Biochemistry 2011, 14;50 (23), 5236-48.
  21. "Kinetic and Spectroscopic Studies of Hemin Acquisition in the Hemophore HasAp from Pseudomonas aeruginosa", Yukl, E.T., Jepkorir G., Alontaga A.Y., Pautsch, L., Rodríguez J.C., Rivera M., Moënne-Loccoz, P., Biochemistry 2010, 49, 6646–6654.
  22. "Structural, NMR Spectroscopic, and Computational Investigation of Hemin Loading in the Hemophore HasAp from Pseudomonas aeruginosa." Jepkorir G, Rodríguez J.C., Rui H., Im W., Lovell S., Battaile K.P., Alontaga A.Y., Yukl E.T., Moënne-Loccoz P., Rivera M., J. Am Chem Soc. 2010, June, 132(28) pp 9857-9872, PMID: 20572666.
  23. "Structural Studies of Bacterioferritin B from Pseudomonas aeruginosa Suggest a Gating Mechanism for Iron Uptake via the Ferroxidase Center", Weeratunga, S.K., Lovell, S., Yao,H., Battaile, K.P., Fischer, C.J., Gee, C., and Rivera, M., Biochemistry, 2010, 49 (6), pp 1160–1175.
  24. "Structural basis for the photoconversion of a phytochrome to the activated Pfr form", Ulijasz, A.T., Cornilescu, C.C., Zhang, J., Rivera, M., Markley, J.L., and Vierstra, R.D., Nature, 2010, January 463(7278), 250-4.
  25. "Cyanochromes Are Blue/Green Light Photoreversible Photoreceptors Defined by a Stable Double Cysteine Linkage to a Phycoviolobilin-type Chromophore", Ulijasz A.T., Cornilescu G., von Stetten D., Cornilescu C., Velazquez Escobar F., Zhang J., Stankey R.J., Rivera M., Hildebrandt P., Vierstra R.D..J Biol Chem. 2009 Oct 23;284(43):29757-72.
  26. "Binding of Pseudomonas aeruginosa Apobacterioferritin-Associated Ferredoxin to Bacterioferritin B Promotes Heme Mediation of Electron Delivery and Mobilization of Core Mineral Iron", Weeratunga, S.K., Gee, C.E., Lovell, S., Zeng, Y., Woodin, C.L. and Rivera, M., Biochemistry 2009, 48, 7420–7431.
  27. "Structural Characterization of the Hemophore HasAp from Pseudomonas aeruginosa: NMR Spectroscopy Reveals Protein-Protein Interactions between Holo-HasAp and Hemoglobin", Alontaga, A., Rodriguez, J., Schönbrunn, E., Becker, A., Funke, T., Yukl, E., Hayashi, T., Stobaugh, J., Moënne-Loccoz, P., and Rivera, M., Biochemistry, 2009, 48 (1), 96-109.
  28. "The Dual Role of Heme as Cofactor and Substrate in the Biosynthesis of Carbon Monoxide", Rivera, M. and Rodriguez, J.C., Met. Ions Life Sci. 2009, 6, 241-293.
  29. "X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP+ Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa", Wang, A., Rodríguez, J. C., Han, H., Schönbrunn, E., and Rivera, M., Biochemistry, 2008, 47, 8080–8093.
  30. "Biochemical and Structural Characterization of Pseudomonas aeruginosa Bfd and FPR: Ferredoxin NADP+ Reductase and Not Ferredoxin Is the Redox Partner of Heme Oxygenase under Iron-Starvation Conditions", Wang, A. , Zeng, Y., Han, H., Weeratunga, S., Morgan, B. Moënne-Loccoz, P., Schönbrunn, E., and Rivera, M., Biochemistry 2007, 46, 12198-12211.
  31. "The Hydrogen-Bonding Network in Heme Oxygenase Also Functions as a Modulator of Enzyme Dynamics: Chaotic Motions upon Disrupting the H-Bond Network in Heme Oxygenase from Pseudomonas aeruginosa, Rodriguez, J.C., Zeng, Y., Wilks, A., and Rivera, M., Journal Am. Chem. Soc. 2007, 129, 11730-11742.
  32. Backbone NMR Assignments and H/D Exchange Studies on the Ferric Azide- and Cyanide-Inhibited Forms of Pseudomonas aeruginosa Heme Oxygenase” Rodriguez, J. C., Wilks, A., & Rivera, M., Biochemistry , 2006, 45(14), 4578-4592
  33. 13C NMR Spectroscopy of Core Heme Carbons as a Simple Tool to Elucidate the Coordination State of Ferric High-Spin Heme Proteins” Alontaga, A. Y., Bunce, R. A., Wilks, A ., & Rivera, M Inorg. Chem., 2006, 45(22), 8876-8881
  34. Influence of point mutations on the flexibility of cytochrome b5: molecular dynamics simulations of holoproteins” Cheng, Q., Benson, D. R., Rivera, M., & Kuczera, K., Biopolymers, 2006, 83(3), 297-312.
  35. "Mitochondrial and Microsomal Ferric b5 Cytochromes Exhibit Divergent Conformational Plasticity in the Context of a Common Fold" Simeonov, M., Altuve, A., Massiah, M.A., Wang, A., Eastman, M.A., Benson, D.R, and Rivera, M. Biochemistry, 2005, 44, 9308-9319.
  36. "The Ferrous Verdoheme Heme Oxygenase Complex is Six-Coordinate and Low-Spin" Damaso, C., Bunce, R. A., Barybin, M. V., Wilks, A., & Rivera, M. J. Am. Chem. Soc., 2005, 127, 17582-17583.
  37. "Enhancing the Stability of Microsomal Cytochrome b5: A Rational Approach Informed by Comparative Studies with the Outer Mitochondrial Membrane Isoform," Sun, N., Wang, A., Cowley, A. B., Altuve, A., Rivera, M. & Benson, D. R. Prot. Eng. Design. Select. 2005, 18, 571-579.
  38. "Divergence in Nonspecific Packing Interactions in the Apo State, and its Possible Role In Functional Stabilization of Mitochondrial and Microsomal Cytochromes b5," Cowley, A., Sun, N. Rivera, M., & Benson, D. R. Biochemistry, 2005, 44, 14606-14615
  39. "Heme Oxidation in a Chimeric Protein of the α-Selective Neisseriae meningitidis Heme Oxygenase with the Distal Helix of the δ-Selective Pseudomonas aeruginosa," Deshmukh, R., Zeng, Y., Furci, L. M., Huang, H.-w., Morgand, B. N., Sander, S., Alontaga, A., Bunce R. A., Moënne-Loccoz, P., Rivera, M. & Wilks A. Biochemistry 2005, 44, 13713-13723.
  40. "Azide-Inhibited Bacterial Heme Oxygenases Exhibit an S = 3/2 (dxz,dyz)3(dxy)1(dz2)1 Spin State: Mechanistic Implications for Heme Oxidation," Zeng, Y., Caignan, G. A., Bunce, R. A., Rodríguez, J. C., Wilks, A. & Rivera, M. J. Am. Chem. Soc. 2005, 127, 9794-9807.
  41. "Expression, Mutagenesis, and Characterization of Recombinant Low-Potential Cytochrome c550 of Photosystem II", Andrews, H., Li, Z., Altuve-Blanco, A., Rivera, M. and Burnap, R. L. Biochemistry 2005, 44, 6092-6100.
  42. "Heme oxygenase, steering dioxygen activation toward heme hydroxylation", Rivera, M. and Zeng, Y. J Inorg. Biochem. 2005, 99, 337-354.
  43. "Reduction of the Ferrous α-Verdoheme-Cytochrome b5 Complex" Damaso, C. O., Rubie, N. D., Moĕnne-Loccoz, P. and Rivera, M. Inorg. Chem. 2004, 43, 8470-8478.
  44. "The Heme Oxygenase(s)-Phytochrome System of Pseudomonas aeruginosa", Wegele, R., Tasler, R., Zeng, Y, Rivera, M. and Frankenberg-Dinkel, N. J Biol. Chem. 2004, 44, 45791-45802.
  45. "Stabilizing roles of residual structure in the empty heme binding pockets and unfolded states of microsomal and mitochondrial apocytochrome b5", Cowley, A. B., Rivera, M. & Benson, D. R. Protein Sci. 2004, 13, 2316-2329.
  46. Resonance Assignments for the Water Soluble Domain of Ferric Rat Liver Outer Mitochondrial Membrane Cytochrome b5.” Massiah, M., Altuve, A. Eastaman, M. A., Caignan, G. A. & Rivera, M. In preparation
  47. Mixed Regioselectivity in the Arg-177 Mutants of Corynebacterium diphtheriae Heme Oxygenase as a Consequence of In-Plane Heme Disorder” Zeng, Y., Deshmukh, R., Caignan, G. A., Bunce, R. A., Rivera, M., & Wilks, A. Biochemistry 2004, 43, 5222-5238.
  48. Recent Developments in the 13C NMR Spectroscopic Analysis of Ferric Hemes and Hemoproteins.” Rivera, M. & Caignan G. A. Analytical and Bioanalytical Chem. 2004, 1464-1483. (Invited).
    Springer-Verlag is the copyright holder. The original publication is available at or at . Please use the appropriate URL and/or DOI for the article. Articles disseminated via SpringerLink are indexed, abstracted and referenced by many abstracting and information services, bibliographic networks, subscription agencies, library networks and consortia.
  49. Mammalian Mitochondrial and Microsomal Cytochromes b5 Exhibit Divergent Structural and Biophysical Characteristics” Altuve, A., Wang, L., Benson, D. R., & Rivera, M. Biochem. Biophys. Res. Commun 2004, 314, 602-609.
  50. The Hydroxide Complex of Pseudomonas aeruginosa Heme Oxygenase as a Model of the Low-Spin Iron(III) Hydroperoxide Intermediate in Heme Catabolism: 13C NMR Spectroscopic Evidence for the Active Participation of the Heme in Macrocycle Hydroxylation” Caignan, G. A., Deshmukh, R., Zeng, Y., Wilks, A., Bunce, R. A., & Rivera M. J. Am. Chem. Soc. 2003, 125, 11842-11852.
  51. "Coupled Oxidation vs Heme Oxygenation: Insights from the Study of Axial Ligand Mutants of Mitochondrial Cytochrome b5” Avila , L., Damaso, C. O., Moënne-Loccoz, P. and Rivera, M. J. Am. Chem. Soc. 2003, 125, 4103-4110.
  52. The oxidation of Heme to β- and δ-biliverdin by Pseudomonas aeruginosa Heme Oxygenase is a Consequence of an Unusual Seating of the Heme” Caignan, G. A., Deshmukh, R., Wilks, A., Zeng, Y., Huang, H-W., Moënne-Loccoz, P., Bunce, R. A., Eastman, M. A., & Rivera, M. J. Am. Chem. Soc., 2002,124, 14879-14892.
  53. Toward Engineering the Stability and Hemin Binding Properties of Microsomal Cytochromes b5 into Rat Outer Mitochondrial Membrane Cytochrome b5: Examining the Influence of Residues 25 and 71” Aaron B. Cowley, A. B., Altuve, A., Kuchment,O., Terzyan, S., Zhang, X., Rivera, M. & Benson, D. R. Biochemistry , 2002, 41, 11566-11581.
  54. Models of the Low-Spin Iron(III) Hydroperoxide Intermediate of Heme Oxygenase: Magnetic Resonance Evidence for Population of the dxy Electronic Ground State at Ambient TemperaturesRivera, M., Caignan, G. A., Astashkin, A. V., Raitsimring, A. M., Shokhireva, T. Kh. & Walker, F. A. J. Am. Chem. Soc. 2002, 124, 6077-608
  55. Probing the Differences Between Rat Liver Outer Mitochondrial Membrane Cytochrome b5 and Microsomal Cytochromes b5,” Altuve, A., Silchenko, S., Kyung-Hoon, L. Kuczera, K. Terzyan, S., Zhang, X., Benson, D.R. & Rivera, M. Biochemistry , 2001, 40, 9469-9483.
  56. Modulation of the Redox Potential in Electron Transfer Proteins: Effects of Complex Formation on the Active Site of Cytochrome b5,” Wirtz, M., Zhang, X., Studer, J. & Rivera, M. Faraday Discuss. 2000, 116, 221-233 (invited).
  57. Oxygen Activation by Axial Ligand Mutants of Mitochondrial Cytochrome b5: Oxidation of Heme to Verdoheme and Biliverdin,” Avila, L, Huang, H., Rodríguez, J. C., Moënne-Loccoz, P. & Rivera, M. J. Am. Chem. Soc. 2000, 122, 7618-7619.
  58. Hemin is kinetically trapped in cytochrome b5 from rat outer mitochondrial membrane,” Silchenko, S., Sippel, M. L., Kuchment, O., Benson, D., Mauk, A. G., Altuve, A., & Rivera, M. Biochem. Biophys. Res. Commun. 2000, 273, 467-472.
  59. Ferredoxin-mediated electrocatalytic dehalogenation of haloalkanes by cytochrome P450cam,” Wirtz, M., Klucik, J. & Rivera, M. J. Am. Chem. Soc. 2000, 122, 1047-1056.
  60. Conformation of ethylhexanoate stabilizer on the surface of CdS nanoparticles,” Diaz, D., Rivera, M., Ni, T., Rodríguez, J. C., Castillo-Blum, S. E., Nagesha, D., Robles, J., Alvarez-Fregoso, O. J., Kotov, N. A. J. Phys. Chem. B 1999, 45, 9854-9858.
  61. An electrochemical study of the factors responsible for modulating the reduction potential of putidaredoxin,” Avila , L., Wirtz, M., Bunce, R. A. & Rivera, M. J. Biol. Inorg. Chem. 1999, 4, 664-674.
  62. “Complete isomer-specific 1H and 13C NMR assignments of the heme resonances arising from both isomeric forms of rat liver outer mitochondrial membrane cytochrome b5,” Rivera, M., Qiu, F., Bunce, R. A., & Stark, R. E. J. Biol. Inorg. Chem. 1999, 4, 87-98.
  63. Conversion of mitochondrial cytochrome b5 into a species capable of performing the efficient coupled oxidation of heme,” Rodríguez, J. C. & Rivera, M. Biochemistry 1998, 37, 13082-13090.
  64. “13C-13C Double quantum coherence experiments applied to a paramagnetic heme active site,” Qiu, F. & Rivera M. The NMR Newsletter 1998, 256-257.
  65. “Efficient coupled oxidation of heme performed by the H63M variant of outer mitochondrial membrane cytochrome b5,” Rodríguez, J. C., Desilva, T., & Rivera, M. Chem. Lett. 1998 353-354.
  66. The reduction potential of cytochrome b5 is modulated by its exposed heme edge,Rivera M., Seetharaman R., Girdhar, D., Wirtz, M. S., Zhang, X., Wang, X., & White, S. Biochemistry 1998, 37, 1485-1494.
  67. An 1H-13C-13C edited 1H NMR experiment for making resonance assignments in the active site of heme proteins,” Qiu, F., Rivera, M., & Stark, R. E. J. Magn. Reson. 1998, 130, 76-81.
  68. Formation of tetramethylene sulfoxide via oxidation of tetrahydrothiophene by Cu(II),” Yanagihara, N., Rivera, M. & Ogura T. Main Group Chem. 1997, 2, 161-163.
  69. “Reductive dehalogenation of carbon tetrachloride carried out by sodium dithionite,” Rodríguez, J. C., & Rivera, M. Chem. Lett. 1997, 1133-1134.
  70. "Synthesis of [1,2-13C]- and [2,3-13C]-labeled δ-Aminolevulinic acid”. Bunce, R. A., Schilling III, C. L., & Rivera, M. J. Labelled Compd. and Radiopharm. 1997, 39, 669-675.
  71. 13C NMR spectroscopic and X-ray crystallographic study of the role played by mitochondrial cytochrome b5 heme propionates in the electrostatic binding to cytochrome c,” Rodríguez-Marañón, M., Qiu, F., Stark, R. E., White, S. P., Zhang, X, Foundling, S. I., Rodríguez, V., Schilling, C. L. III, Bunce, R. A., & Rivera, M. Biochemistry 1996, 35, 16378-16390.
  72. “A new 1H-13C-13C filtered 1H NMR experiment for making resonance assignments on the active site of heme proteins,” Qiu Feng, Stark, R. E., & Rivera M. NMR Newsletter 1996, 5-6.
  73. Electrochemical measurement of second order electron transfer rate constants for the reaction between cytochrome b5 and cytochrome c,” Seetharaman, R., White, S. P., & Rivera M. Biochemistry 1996, 35, 12455-12463.
  74. Biosynthesis of isotopically enriched protohemin IX.Rivera, M. & Walker, F. A. Anal. Biochem. 1995, 230, 295-302.
  75. Hydration and localization of diacylglycerol in the insect lipoprotein, lipophorin. A 13C-NMR study,” Soulages, J. L., Rivera, M., Walker, F. A., & Wells, M. A. Biochemistry 1994, 33, 3245-3251.
  76. Cation promoted cyclic voltammetry of recombinant rat outer mitochondrial membrane cytochrome b5 at a gold electrode modified with β-mercaptopropionic Acid,” Rivera, M., Wells, M. A., & Walker, F. A. Biochemistry 1994, 33, 2161-2170.
  77. Cyclic voltammetric studies of recombinant rat outer mitochondrial membrane cytochrome b5,Rivera M. J. Inorg. Biochem. 1993, 51, 132.
  78. Laser flash photolysis studies of electron transfer to the cytochrome b5- cytochrome c complex.” Meyer, T. E., Rivera, M., Walker , F. A., Mauk, A. G., Cusanovich, M. A., & Tollin, G. Biochemistry 1993, 32, 622-627.
  79. Gene Synthesis, Bacterial Expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5,Rivera, M., Barillas-Mury, C., Christensen, K., Little, J. W., Wells, M. A., & Walker, F. A. Biochemistry 1992, 31, 12233-12240.
  80. Determination and metabolism of dithiol chelating agents. XIV. The zinc chelate of the dimethyl ester of meso-2,3-dimercaptosuccinic acid increases the biliary excretion of cadmium and platinum,” Aposhian, H. V., Levine, D. J., Rivera, M., & Fernando, Q. Chem. Res. Toxicol. 1993, 6, 208-214.
  81. Human studies with the chelating agents DMPS and DMSA,” Aposhian, H. V., Maiorino, R. M., Rivera, M., Bruce, D. C., Dart, R. C., Hurlbut, K. M., Levine, D. J., Zheng, W., Fernando, Q., Carter, D., & Aposhian, M. M Clinical Toxicol. 1992, 30, 505-528.
  82. A synthetic method for unsymmetrical disulfides of cysteine: “The bis-cysteine disulfide of meso-2,3-dimercaptosuccinic acid,” Polt, R., Li, Y., Fernando, Q., & Rivera, M. Tetrahedron. Letters 1992, 33, 2961-2964.
  83. Synthesis, Structure and stability of the zinc complex of the dimethyl ester of meso-2,3-dimercaptosuccinic Acid, [(Me4)2[Zn(DiMeDMSA)2],” Rivera, M., & Fernando, Q. Chem. Res. Toxicol. 1992, 5, 142-147.
  84. The dimethyl ester of meso-2,3-dimercaptosuccinic acid and its interactions with Cd2+ and rabbit liver metallothionein I,Rivera, M., Bruck, M. A., Aposhian, H. V., & Fernando, Q. Chem. Res. Toxicol. 1991, 4, 572-580.
  85. Synthesis and properties of the monomethyl ester of meso-dimercaptosuccinic acid and its chelates of lead(II) cadmium(II) and mercury(II),Rivera, M., Levine, D. J., Aposhian, H. V., & Fernando, Q. Chem. Res. Toxicol. 1991, 4, 107-114.
  86. Lead chelates of meso- and racemic-dimercaptosuccinic acid, “Rivera, M., Aposhian, H. V., & Fernando, Q. J. Inorg. Biochem. 1989, 37, 283-293.
  87. “Determination and metabolism of dithiol chelating agents VIII. Metal complexes of meso-dimercaptosuccinic acid,” Rivera, M., Zheng, W., Aposhian, H. V., & Fernando, Q. Toxicol. Appl. Pharmacol. 1989, 100, 96-106.

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