Publications

Hines, J.P.; Dent, M.R.; Stevens, D.J.; Burstyn, J.N. Site-Directed Spin Label Electron Paramagnetic Resonance Spectroscopy as a Probe of Conformational Dynamics in the Fe(III) “Locked-Off” State of the CO-Sensing Transcription Factor CooA. Prot. Sci. 2018, 27, 1670-1679.

Hines, J. P.; Smith, A. T.; Jacob, J. P.; Lukat-Rodgers, G. S.; Barr, I.; Rodgers, K. R.; Guo, F.; Burstyn, J. N. “CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity”. J. Biol. Inorg. Chem. 2016. 21, 1021.

Bowman, H.E.; Dent, M.R.; Burstyn, J.N. “Met¹⁰⁴ is the CO-replaceable Ligand at Fe(II) Heme in the CO-sensing Transcription Factor BxRcoM-1″ J. Biol. Inorg. Chem. 2016. 21, 1-11.

Tanimura, N.; Miller, E.; Igarashi, K.; Yang, D.; Burstyn, J.N.; Dewey, C.N.; Bresnick, E.H. “Mechanism Governing Heme Synthesis Reveals a GATA Factor/Heme Circuit that Controls Differentiation”. EMBO Reports. 2016. 17, 249-265.

Smith, A.T.; Pazicni, S.; Marvin, K.A.; Stevens, D.J.; Paulsen, K.M.; Bursty, J.N. “Functional Divergence of Heme-Thiolate Proteins: A Classification Based on Spectroscopic Attributes”. Chemical Reviews. 2015, 115(7), 2532-2558.

Su, Y.; Majtan, T.; Freeman, K.M.; Linck, R.C.; Ponter, S.; Kraus, J.P.; Burstyn, J.N. “Comparative Study of Enzyme Activity and Heme Reactivity in Drosophila melanogaster and Homo sapiens Cystathionine beta-Synthases.” Biochemistry. 2013, 52(4), 741-751.

Smith, A.T.; Marvin, K.A.; Freeman, K.M.; Kerby, R.L.; Roberts, G.P.; Burstyn, J.N. “Identification of Cys94 as the Distal Ligand to the Fe(III) Heme in the Transcriptional Regulator RcoM-2 from Burkholderia xenovorans“. J. Biol. Inorg. Chem.2012, 17, 1071-1082.

Smith, A.T.; Su, Y.; Stevens, D.J.; Majtan, T.; Kraus, J.P.; Burstyn, J.N. “Effect of the Disease-Causing R266K Mutation on the Heme and PLP Environments of Human Cystathionine ß-Synthase”. Biochemistry. 2012, 51 (32), pp 6360–6370.

Santiago Cintrón, M.; Green, O.; Burstyn, J.N. “Ethylene Sensing by Silver(I) Salt-Impregnated Luminescent Films”. Inorg. Chem. 2012, 51 (5), 2737–2746.

Barr, I.; Smith, A. T.; Chen, Y.; Senturia, R.; Burstyn, J. N.; Guo, F. “Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing.” Proc. Natl. Acad. Sci. U.S.A., 2012, 109, 1919-1924.

Smith, A.T.; Majtan, T.;  Freeman, K.M.; Su, Y.; Kraus, J.P.; Burstyn, J.N. “Cobalt Cystathionine β-Synthase: A Cobalt-Substituted Heme Protein with a Unique Thiolate Ligation Motif”. Inorg. Chem. 2011, 50, 4417-4427.

Barr, I.; Smith, A.T.; Senturia, R.; Chen, Y.; Burstyn, J.N.; Guo, F. “DiGeorge Critical Region 8 (DGCR8) Is a Double-Cysteine-Ligated Heme Protein”. J. Biol. Chem. 2011, 286, 16716-16725.

Majtan, T., Freeman, K. M., Smith, A. T., Burstyn, J. N., Kraus, J. P. “Purification and characterization of cystathionine β-synthase bearing a cobalt protoporphyrin” Arch. Biochem. Biophys., 2011, 508, 25-30.

Ostrowski, A. D., Deakin, S. J, Azhar, B., Miller, T. W., Francoleon, N., Cherney, M. M., Lee, A., Burstyn, J. N., Fukuto, J. M., Megson, I. L., Ford, P. C. “Nitric Oxide Photogeneration from trans-Cr(cyclam)(ONO)₂⁺ in a Reducing Environment. Activation of Soluble Guanylyl Cyclase and Arterial Vasorelaxation” J. Med. Chem., 2010, 53, 715-722.

2000-2009

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Miller, T. W., Cherney, M. M., Lee, A. J., Francoleon, N. E., Farmer, P. J., Bruce King, S., Hobbs, A. J., Miranda, K. M., Burstyn, J. N., Fukuto, J. M. “The effects of nitroxyl (HNO) on soluble guanylyl cyclase activity: Interactions at ferrous heme and cysteine thiols” J. Biol. Chem., 2009, 284, 21788-21796.

Marvin, K. A., Reinking, J. L., Lee, A. J., Pardee, K., Krause, H. M., Burstyn, J. N. “Nuclear receptors Homo sapiens Rev-erb beta and Drosophila melanogaster E75 are thiolate-ligated heme proteins, which undergo redox-mediated ligand switching and bind CO and NO” Biochemistry, 2009, 48, 7056–7071.

Green, O., Gandhi, B. A., Burstyn, J. N. “Photophysical Characteristics and Reactivity of Bis(2,9-di-tert-butyl-1,10-phenanthroline)Cu(I)” Inorg. Chem., 2009, 48, 5704–5714.

Lee, A. J., Clark, R. W., Youn, H., Ponter, S., Burstyn, J. N. “Guanidine Hydrochloride-Induced Unfolding of the Three Heme Coordination States of the CO-Sensing Transcription Factor, CooA” Biochemistry, 2009, 48, 6585-6597.

Tseng, T. A., Burstyn, J. N. “Synthesis and DNA Cleavage Activity of a Bifunctional Intercalator-Linked Copper(II) Macrocycle” Chem. Commun., 2008, 6209-6211.

Marvin, K. A., Kerby, R. L., Youn, H., Roberts, G. P., Burstyn, J. N. “The CO-activated transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch” Biochemistry, 2008, 47, 9016-9028.

Cherney, M. M., Pazicni, S., Frank, N., Marvin, K. A., Kraus, J. P., Burstyn, J. N. “Ferrous Human Cystathionine β-Synthase Loses Activity during Enzyme Assay Due to a Ligand Switch Process.” Biochemistry, 2007, 46, 13199-13210.

Gandhi, B. A., Green, O., Burstyn, J. N. “Facile Oxidation-Based Synthesis of Sterically Encumbered Four-Coordinate Bis(2,9-di-tert-butyl-1,10-phenanthroline)copper(I) and Related Three-Coordinate Copper(I) Complexes.” Inorganic Chemistry 2007, 46, 3816-3825.

Clark,R. W., Youn, H., Lee, A. J., Roberts, G. P., Burstyn, J. N. “DNA binding by an imidazole-sensing CooA variant is dependent on the heme redox state.” Journal of Biological Inorganic Chemistry 2007, 12, 139-146.

Pinkert, J. C., Clark, R. W., Burstyn, J. N. “Modeling proline ligation in the heme-dependent CO sensor, CooA, using molecule analogs.” Journal of Biological Inorganic Chemistry 2006, 11, 642-650.

Clark, R. W., Lanz, N. D., Lee, A. J., Kerby, R. L., Roberts, G. P., Burstyn, J. N. “Unexpected NO-dependent DNA binding by the CooA homolog from Carboxydothermus hydrogenoformans.” Proceedings of the National Academy of Sciences USA, 2006, 103, 891-896.

Pazicni, S., Cherney, M. M., Lukat-Rogers, G. S., Oliveriusová, J., Rodgers, K. R., Kraus, J. P., Burstyn, J. N. “The Heme of Cystathionine β-synthase Likely Undergoes a Thermally Induced Redox-Mediated Ligand Switch.” Biochemistry, 2005, 44, 16785-16795.

Pazicni, S., Lukat-Rodgers, G. S., Oliveriusová, J., Rees, K. A., Parks, R. B., Clark, R. W., Kraus, J., Rodgers, K. R., and Burstyn, J. N. “The redox behavior of the heme in cystathionine β-synthase is sensitive to pH.” Biochemistry 2004, 43, 14684-14695.

Clark, R. W., Youn, H., Parks, R. B., Cherney, M. M., Roberts, G. P., and Burstyn, J. N. “Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA.” Biochemistry 2004, 43, 14149-14160.

Green, O., Smith, N. A., Ellis, A. B., Burstyn, J. N. “AgBF₄-Impregnated poly(vinyl phenyl ketone): An Ethylene Sensing Film.” Journal of the American Chemical Society 2004, 126, 5952-5953.

Youn, H., Kerby, R. L., Thorsteinsson, M. V., Clark, R. W., Burstyn, J. N., Roberts, G. P. “Analysis of the L116K Variant of CooA, the Heme-containing CO Sensor, Suggest the Presence of an Unusual Heme Ligation Resulting in Novel Activity.” Journal of Biological Chemistry 2002, 277, 33616-33623.

Amin, S., Chappell, L. L., Morrow, J. R., Tseng, T. A., Bodsgard, B. R., Burstyn, J. N. “Compounds of general interest. Preparation of a synthetic ribonuclease: the europium(III) complex of 1-(4-nitrobenzyl)-4,7,10-tris(carbamoylmethyl)-1,4,7,10-tetraazacyclododecane.” Inorganic Syntheses 2002, 33, 213-218.

Carr, H. S., Tran, D., Reynolds, M. F., Burstyn, J. N., Spiro, T. G. “Activation of soluble guanylyl cyclase by four-coordinate metalloporphyrins: evidence for a role for porphyrin conformation.” Biochemistry 2002, 41, 10149-10157.

Deck, K. M., Tseng, T. A., Burstyn, J. N. “Triisopropyltriazacyclononane Copper(II): An Efficient Phosphodiester Hydrolysis Catalyst and DNA Cleavage Agent.” Inorganic Chemistry 2002, 41, 669-677.

Richter-Addo, G. B., Legzdins, P., Burstyn, J. “Introduction: Nitric Oxide Chemistry.” Chemical Reviews 2002, 102, 857-860.

Hirsch, J., DeBeer George, S., Solomon, E. I., Hedman, B., Hodgson, K. O., Burstyn, J. N. “Raman and Extended X-ray Absorption Fine Structure Characterization of a Sulfur-Ligated Cu(I) Ethylene Complex: Modeling the Proposed Ethylene Binding Site of Arabidopsis thaliana ETR1.” Inorganic Chemistry 2001, 40, 2439-2441.

Serfass, L., Carr, H. S., Aschenbrenner, L. M., Burstyn, J. N. “Calcium ion down regulates soluble guanylyl cyclase activity: Evidence for a second metal ion binding site.” Archives of Biochemistry and Biophysics 2001, 387, 47-56.

Bodsgard, B. R., Burstyn, J. N. “Silica-bound copper(II)triazacyclononane: a robust material for the heterogeneous hydrolysis of a phosphodiester.” Chemical Communications 2001, 7, 647-648.

Polzin, G. M., Burstyn, J. N. “Synthetic Cu(II) and Ni(II) peptidases,” in Metal Ions in Biological Systems: Probing of Proteins by Metal Ions and Their Low-Molecular Weight Complexes, Vol. 38 (Astrid and Helmut Sigel, Eds.) 2000, pp. 103-143, Marcel Decker, New York.

Reynolds, M. F., Burstyn, J. N. “Mechanism of activation of soluble guanylyl cyclase by NO: allosteric regulation through changes in heme coordination geometry” in Nitric Oxide: Biology and Pathobiology (Louis Ignarro, Ed.) 2000, pp. 381-399, Academic Press, San Diego.

Ivanisevic, A., Reynolds, M. F., Burstyn, J. N., Ellis, A. B. “Photoluminescent Properties of Cadmium Selenide in Contact with Solutions and Films of Metalloporphyrins: Nitric Oxide Sensing and Evidence for the Aversion of an Analyte to a Buried Semiconductor-Film Interface” Journal of the American Chemical Society 2000, 122, 3731-3738.

Reynolds, M. F., Parks, R. B., Burstyn, J. N., Shelver, D., Thorsteinsson, M. V., Kerby, R. L., Roberts, G. L., Vogel, K. M., Spiro, T. G. “Electronic absorption, EPR and resonance Raman spectroscopies of CooA, a CO-sensing transcription activator from R. rubrum, reveal a five-coordinate NO-heme.” Biochemistry 2000, 39, 388-396.

Kavana, M., Powell, D. R., Burstyn, J. N. “Static versus dynamic Jahn-Teller distortions in octahedral-like copper(II) complexes of 1,4,7-triazacyclononane and 1-oxa-4,7-diazacyclononane: implications for hydrolytic reactivity.” Inorganica Chimica Acta 2000, 297, 351-361.

1990-1999

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Vogel, K. M., Hu, S., Spiro, T. G., Dierks, E. A., Yu, A. E., Burstyn, J. N. “Variable forms of soluble guanylyl cyclase (sGC): protein ligand interactions and the issue of activation by CO.” Journal of Biological Inorganic Chemistry 1999, 4, 804-813.

Shelver, D., Thorsteinsson, M. V., Chung, S.-Y., Roberts, G. P., Reynolds, M. F., Parks, R. B., Burstyn, J. N. “Identification of two important heme site residues (Cys⁷⁵ and His⁷⁷) in CooA, the CO-Sensing transcription factor of Rhodospirillum rubrum.” Biochemistry 1999, 38, 2669-2678.

Hegg, E. L., Mortimore, S. H., Cheung, C.-L., Huyett, J. E., Powell, D. R., Burstyn, J. N. “Structure-reactivity studies in Cu(II)-catalyzed phosphodiester hydrolysis.” Inorganic Chemistry 1999, 38, 2961-2968.

Reynolds, M. F., Burstyn, J. N. “Nitric Oxide.” McGraw Hill 1999 Yearbook of Science and Technology 1999, 255-256.

Hegg, E. L, Burstyn, J. N. “Toward the development of metal-based synthetic nucleases and proteases: a rationale and progress report in applying the principles of coordination chemistry.” Coordination Chemistry Reviews 1998, 173, 133-165.

Reynolds, M.F., Shelver, D., Kerby, R. L., Parks, R. B., Roberts, G. P., Burstyn, J. N. “EPR and Electronic Absorption Spectroscopies of the CO-sensing CooA Protein Reveal a Cysteine-Ligated Low-Spin Ferric Heme.” Journal of the American Chemical Society 1998, 120, 9080-9081.

Serfass, L., Burstyn, J. N. “Effect of heme oxygenase inhibitors on soluble guanylyl cyclase activity.” Archives of Biochemistry and Biophysics 1998, 359, 8-16.

Dierks, E. A., Burstyn, J. N. “Deactivation of soluble guanylyl cyclase by redox active agents.” Archives of Biochemistry and Biophysics 1998, 351, 1-7.

Hegg, E. L., Deal, K. A., Kiessling, L. L., Burstyn, J. N. “Hydrolysis of double-stranded and single-stranded RNA in hairpin structures by the copper(II) macrocycle Cu([9]aneN₃)Cl₂.” Inorganic Chemistry 1997, 36, 1715-1718.

Dierks, E. A., Hu, S., Yu, A.., Spiro, T. G., Burstyn, J. N. “Demonstration of the role of scission of the proximal histidine-iron bond in the activation of soluble guanylyl cyclase through metalloporphyrin substitution studies.” Journal of the American Chemical Society 1997, 119, 7316-7323.

Hegg, E. L., Burstyn, J. N. “Copper(II) macrocycles cleave single-stranded and double-stranded DNA under both aerobic and anaerobic conditions.” Inorganic Chemistry 1996, 35, 7474-7481.

Deal, K. A., Hengge, A. C., Burstyn, J. N. “Characterization of Transition States in Dichloro(1,4,7-triazacyclononane)copper(II)-Catalyzed Activated Phosphate Diester Hydrolysis.” Journal of the American Chemical Society1996, 118, 1713-1718.

Deal, K. A., Burstyn, J. N. “Mechanistic studies of dichloro(1,4,7-triazacyclononane)copper(II)- catalyzed phosphate diester hydrolysis.” Inorganic Chemistry 1996, 35, 2792-2798.

Dierks, E. A., Burstyn, J. N. “Nitric oxide (NO·), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase.” Biochemical Pharmacology 1996, 51, 1593-1600.

Hegg, E. L., Burstyn, J. N. “Hydrolysis of Unactivated Peptide Bonds by a Macrocyclic Copper(II) Complex: Cu([9]aneN₃)Cl₂Hydrolyzes Both Dipeptides and Proteins.” Journal of the American Chemical Society 1995, 117, 7015-7016.

Yu, A. E., Hawkins, B. K., Dierks, E. A.., Dawson, J. H., Burstyn, J. N. “Studies of the heme binding environment and ligand binding properties of soluble guanylyl cyclase: characterization of Fe(II)sGC and Fe(II)sGC(CO) by electronic absorption and magnetic circular dichroism spectroscopies and failure of CO to activate the enzyme.” Biochemistry 1995, 34, 5896-5903.

Kim, T. D., Burstyn, J. N. “Identification and partial purification of an endogenous regulator of soluble guanylyl cyclase from bovine lung.” Journal of Biological Chemistry 1994, 269, 15540-15545.

Yu, A. E., Hu, S., Spiro, T. G., Burstyn, J. N. “Resonance Raman Spectroscopy of Soluble Guanylyl Cyclase Reveals Displacement of Distal and Proximal Heme Ligands by NO.” Journal of the American Chemical Society 1994, 116, 4117-4118.

Burstyn, J. N., Deal, K. A. “Selective catalytic hydrolysis of a simple phosphodiester by a macrocyclic copper(II) complex.” Inorganic Chemistry 1993, 32, 3585-3586.