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Publications


(to receive a copy of any of these publications, please send an email to mrivera@ku.edu)

A. From Ph. D. Research:

  1. “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.
  2. “Lead chelates of meso- and racemic-dimercaptosuccinic acid, “Rivera, M., Aposhian, H. V., & Fernando, Q. J. Inorg. Biochem. 1989, 37, 283-293.
  3. “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.
  4. “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.
  5. “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.
  6. “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.
  7. “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.
  8. “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.

B. From Postdoctoral Work:

  1. “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.
  2. “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.
  3. “Cyclic voltammetric studies of recombinant rat outer mitochondrial membrane cytochrome b5,” Rivera M. J. Inorg. Biochem. 1993, 51, 132.
  4. “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.
  5. “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.

C. From Research Done at Oklahoma State University:

  1. “Biosynthesis of isotopically enriched protohemin IX.” Rivera, M. & Walker, F. A. Anal. Biochem. 1995, 230, 295-302.
  2. “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.
  3. “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.
  4. “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.
  5. "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.
  6. “Reductive dehalogenation of carbon tetrachloride carried out by sodium dithionite,” Rodríguez, J. C., & Rivera, M. Chem. Lett. 1997, 1133-1134.
  7. “Formation of tetramethylene sulfoxide via oxidation of tetrahydrothiophene by Cu(II),” Yanagihara, N., Rivera, M. & Ogura T. Main Group Chem. 1997, 2, 161-163.
  8. “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.
  9. “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.
  10. “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.
  11. “13C-13C Double quantum coherence experiments applied to a paramagnetic heme active site,” Qiu, F. & Rivera M. The NMR Newsletter 1998, 256-257.
  12. “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.
  13. “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.
  14. “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.
  15. “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.
  16. “Ferredoxin-mediated electrocatalytic dehalogenation of haloalkanes by cytochrome P450cam,” Wirtz, M., Klucik, J. & Rivera, M. J. Am. Chem. Soc. 2000, 122, 1047-1056.
  17. “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.
  18. “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.
  19. “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).
  20. “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.
  21. “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 Temperatures” Rivera, M., Caignan, G. A., Astashkin, A. V., Raitsimring, A. M., Shokhireva, T. Kh. & Walker, F. A. J. Am. Chem. Soc. 2002, 124, 6077-608
  22. “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.
  23. “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.
  24. "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.

D. From Research Done at the University of Kansas:

  1. “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.
  2. “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.
  3. “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).

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  1. 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.
  2. “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
  3. "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.
  4. "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.
  5. "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.
  6. "Heme oxygenase, steering dioxygen activation toward heme hydroxylation", Rivera, M. and Zeng, Y. J Inorg. Biochem. 2005, 99, 337-354.
  7. "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.
  8. "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.
  9. "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.
  10. "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
  11. "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.
  12. "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.
  13. "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.
  14. “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.
  15. 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
  16. “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
  17. "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.
  18. "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. J., Biochemistry 2007, 46, 12198-12211.
  19. "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. J., Biochemistry, 2008, 47, 8080–8093.