Publications

Publications List with Links

2010-Present


Dent, M.R.; Milbauer, M.W.; Hunt, A.P.; Aristov, M.M.; Guzei, I.A.; Lehnert, N.; Burstyn, J.N. Electron Paramagnetic Resonance Spectroscopy as a Probe of Hydrogen Bonding in Heme-Thiolate Proteins. Inorg. Chem. 2019, 58, 16011-16027.

Tanimura, N.; Liao, R.; Wilson, G.M.; Dent, M.R.; Cao, M.; Burstyn, J.N.; Hematti, P.; Liu, X.; Zhang, Y.; Zheng, Y.; Keles, S.; Xu, J.; Coon, J.J.; Bresnick, E.H. GATA/Heme Multi-omics Reveals a Trace Metal-Dependent Cellular Differentiation Mechanism. Dev. Cell 201846, 1-14.

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. 201827, 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. 201621, 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 Reports2016. 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.” Biochemistry201352(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.201217, 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. 201251 (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.2012109, 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. 201150, 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. 2011286, 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.201053, 715-722.

2000-2009


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.2009284, 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” Biochemistry200948, 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.200948, 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” Biochemistry200948, 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” Biochemistry200847, 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.” Biochemistry200746, 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 200746, 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 200712, 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 200611, 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 USA2006103, 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.” Biochemistry200544, 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 200443, 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 200443, 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 2004126, 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 2002277, 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 200233, 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 200241, 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 200241, 669-677.

Richter-Addo, G. B., Legzdins, P., Burstyn, J. “Introduction: Nitric Oxide Chemistry.” Chemical Reviews 2002102, 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 200140, 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 2001387, 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 20017, 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 2000122, 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 200039, 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 2000297, 351-361.

1990-1999


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 19994, 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 199938, 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 199938, 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 1998173, 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 1998120, 9080-9081.

Serfass, L., Burstyn, J. N. “Effect of heme oxygenase inhibitors on soluble guanylyl cyclase activity.” Archives of Biochemistry and Biophysics 1998359, 8-16.

Dierks, E. A., Burstyn, J. N. “Deactivation of soluble guanylyl cyclase by redox active agents.” Archives of Biochemistry and Biophysics 1998351, 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 199736, 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 1997119, 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 199635, 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 Society1996118, 1713-1718.

Deal, K. A., Burstyn, J. N. “Mechanistic studies of dichloro(1,4,7-triazacyclononane)copper(II)- catalyzed phosphate diester hydrolysis.” Inorganic Chemistry 199635, 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 199651, 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 1995117, 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 199534, 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 1994269, 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 1994116, 4117-4118.

Burstyn, J. N., Deal, K. A. “Selective catalytic hydrolysis of a simple phosphodiester by a macrocyclic copper(II) complex.” Inorganic Chemistry 199332, 3585-3586.