Johnson, A.R., Rao, K., Zhang, B.B., Mullet, S., Goetzman, E., Gelhaus, S., Tejero, J., & Shiva, U. (2024). Myoglobin Inhibits Breast Cancer Cell Fatty Acid Oxidation and Migration via Heme-dependent Oxidant Production and Not Fatty Acid Binding. bioRxiv, 2024.04.30.591659.Cold Spring Harbor Laboratory. doi: 10.1101/2024.04.30.591659.
Kaminski, T.W., Sivanantham, A., Mozhenkova, A., Smith, A., Ungalara, R., Dubey, R.K., Shrestha, B., Hanway, C., Katoch, O., Tejero, J., Sundd, P., Novelli, E.M., Kato, G.J., & Pradhan-Sundd, T. (2024). Hemoglobin scavenger receptor CD163 as a potential biomarker of hemolysis-induced hepatobiliary injury in sickle cell disease. Am J Physiol Cell Physiol, 327(2), C423-C437.American Physiological Society. doi: 10.1152/ajpcell.00386.2023.
DeMartino, A.W., Poudel, L., Dent, M.R., Chen, X., Xu, Q., Gladwin, B.S., Tejero, J., Basu, S., Alipour, E., Jiang, Y., Rose, J.J., Gladwin, M.T., & Kim-Shapiro, D.B. (2023). Thiol-catalyzed formation of NO-ferroheme regulates intravascular NO signaling. Nat Chem Biol, 19(10), 1256-1266.Springer Nature. doi: 10.1038/s41589-023-01413-3.
DeMartino, A.W., Poudel, L., Dent, M.R., Chen, X., Xu, Q., Gladwin, B.S., Tejero, J., Basu, S., Alipour, E., Jiang, Y., Rose, J.J., Gladwin, M.T., & Kim-Shapiro, D.B. (2023). Thiol catalyzed formation of NO-ferroheme regulates canonical intravascular NO signaling. Res Sq, rs.3.rs-2402224.Research Square Platform. doi: 10.21203/rs.3.rs-2402224/v1.
Tejero, J. (2023). Artificial porphyrin molecules clean up carbon monoxide and cyanide. Proc Natl Acad Sci U S A, 120(11), e2301732120.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.2301732120.
Hernandez-Berthet, A.S., Aptekmann, A.A., Tejero, J., Sánchez, I.E., Noguera, M.E., & Roman, E.A. (2022). PhISCO: a simple method to infer phenotypes from protein sequences. 2022.10.23.511734.Cold Spring Harbor Laboratory. doi: 10.1101/2022.10.23.511734.
Vats, R., Kaminski, T.W., Brzoska, T., Leech, J.A., Tutuncuoglu, E., Katoch, O., Jonassaint, J., Tejero, J., Novelli, E.M., Pradhan-Sundd, T., Gladwin, M.T., & Sundd, P. (2022). Liver-to-lung microembolic NETs promote gasdermin D-dependent inflammatory lung injury in sickle cell disease. Blood, 140(9), 1020-1037.American Society of Hematology. doi: 10.1182/blood.2021014552.
Dent, M.R., DeMartino, A.W., Tejero, J., & Gladwin, M.T. (2021). Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite. Inorg Chem, 60(21), 15918-15940.American Chemical Society (ACS). doi: 10.1021/acs.inorgchem.1c01048.
Olonisakin, T.F., Suber, T., Gonzalez-Ferrer, S., Xiong, Z., Peñaloza, H.F., van der Geest, R., Xiong, Y., Osei-Hwedieh, D.O., Tejero, J., Rosengart, M.R., Mars, W.M., Van Tyne, D., Perlegas, A., Brashears, S., Kim-Shapiro, D.B., Gladwin, M.T., Bachman, M.A., Hod, E.A., St Croix, C., Tyurina, Y.Y., Kagan, V.E., Mallampalli, R.K., Ray, A., Ray, P., & Lee, J.S. (2021). Stressed erythrophagocytosis induces immunosuppression during sepsis through heme-mediated STAT1 dysregulation. J Clin Invest, 131(1), 137468.American Society for Clinical Investigation. doi: 10.1172/JCI137468.
Vats, R., Kaminski, T.W., Ju, E.M., Brozska, T., Tutuncuoglu, E., Tejero, J., Novelli, E.M., Sundd, P., & Pradhan-Sundd, T. (2021). P-selectin deficiency promotes liver senescence in sickle cell disease mice. Blood, 137(19), 2676-2680.American Society of Hematology. doi: 10.1182/blood.2020009779.
Wang, J., Applefeld, W.N., Sun, J., Solomon, S.B., Feng, J., Couse, Z.G., Risoleo, T.F., Danner, R.L., Tejero, J., Lertora, J., Alipour, E., Basu, S., Sachdev, V., Kim-Shapiro, D.B., Gladwin, M.T., Klein, H.G., & Natanson, C. (2021). Mechanistic insights into cell-free hemoglobin-induced injury during septic shock. Am J Physiol Heart Circ Physiol, 320(6), H2385-H2400.American Physiological Society. doi: 10.1152/ajpheart.00092.2021.
Rochon, E.R., Missinato, M.A., Xue, J., Tejero, J., Tsang, M., Gladwin, M.T., & Corti, P. (2020). Nitrite Improves Heart Regeneration in Zebrafish. Antioxid Redox Signal, 32(6), 363-377.Mary Ann Liebert. doi: 10.1089/ars.2018.7687.
Tejero, J. (2020). Negative surface charges in neuroglobin modulate the interaction with cytochrome c. Biochem Biophys Res Commun, 523(3), 567-572.Elsevier. doi: 10.1016/j.bbrc.2019.12.089.
Wang, L., Sparacino-Watkins, C.E., Wang, J., Wajih, N., Varano, P., Xu, Q., Cecco, E., Tejero, J., Soleimani, M., Kim-Shapiro, D.B., & Gladwin, M.T. (2020). Carbonic anhydrase II does not regulate nitrite-dependent nitric oxide formation and vasodilation. Br J Pharmacol, 177(4), 898-911.Wiley. doi: 10.1111/bph.14887.
Amdahl, M.B., Petersen, E.E., Bocian, K., Kaliszuk, S.J., DeMartino, A.W., Tiwari, S., Sparacino-Watkins, C.E., Corti, P., Rose, J.J., Gladwin, M.T., Fago, A., & Tejero, J. (2019). The Zebrafish Cytochrome b5/Cytochrome b5 Reductase/NADH System Efficiently Reduces Cytoglobins 1 and 2: Conserved Activity of Cytochrome b5/Cytochrome b5 Reductases during Vertebrate Evolution. Biochemistry, 58(29), 3212-3223.American Chemical Society (ACS). doi: 10.1021/acs.biochem.9b00406.
Tejero, J., Hunt, A.P., Santolini, J., Lehnert, N., & Stuehr, D.J. (2019). Mechanism and regulation of ferrous heme-nitric oxide (NO) oxidation in NO synthases. J Biol Chem, 294(19), 7904-7916.Elsevier. doi: 10.1074/jbc.RA119.007810.
Tejero, J., Shiva, S., & Gladwin, M.T. (2019). Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation. Physiol Rev, 99(1), 311-379.American Physiological Society. doi: 10.1152/physrev.00036.2017.
Haque, M.M., Tejero, J., Bayachou, M., Kenney, C.T., & Stuehr, D.J. (2018). A cross-domain charge interaction governs the activity of NO synthase. J Biol Chem, 293(12), 4545-4554.Elsevier. doi: 10.1074/jbc.RA117.000635.
Qu, Y., Olonisakin, T., Bain, W., Zupetic, J., Brown, R., Hulver, M., Xiong, Z., Tejero, J., Shanks, R.M., Bomberger, J.M., Cooper, V.S., Zegans, M.E., Ryu, H., Han, J., Pilewski, J., Ray, A., Cheng, Z., Ray, P., & Lee, J.S. (2018). Thrombospondin-1 protects against pathogen-induced lung injury by limiting extracellular matrix proteolysis. JCI Insight, 3(3), e96914.American Society for Clinical Investigation. doi: 10.1172/jci.insight.96914.
Wang, B., Shi, Y., Tejero, J., Powell, S.M., Thomas, L.M., Gladwin, M.T., Shiva, S., Zhang, Y., & Richter-Addo, G.B. (2018). Nitrosyl Myoglobins and Their Nitrite Precursors: Crystal Structural and Quantum Mechanics and Molecular Mechanics Theoretical Investigations of Preferred Fe -NO Ligand Orientations in Myoglobin Distal Pockets. Biochemistry, 57(32), 4788-4802.American Chemical Society (ACS). doi: 10.1021/acs.biochem.8b00542.
Amdahl, M.B., DeMartino, A.W., Tejero, J., & Gladwin, M.T. (2017). Cytoglobin at the Crossroads of Vascular Remodeling. Arterioscler Thromb Vasc Biol, 37(10), 1803-1805.Wolters Kluwer. doi: 10.1161/ATVBAHA.117.310058.
Amdahl, M.B., Sparacino-Watkins, C.E., Corti, P., Gladwin, M.T., & Tejero, J. (2017). Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b5/Cytochrome b5 Reductase/NADH System. Biochemistry, 56(30), 3993-4004.American Chemical Society (ACS). doi: 10.1021/acs.biochem.7b00224.
Eshbach, M.L., Kaur, A., Rbaibi, Y., Tejero, J., & Weisz, O.A. (2017). Hemoglobin inhibits albumin uptake by proximal tubule cells: implications for sickle cell disease. Am J Physiol Cell Physiol, 312(6), C733-C740.American Physiological Society. doi: 10.1152/ajpcell.00021.2017.
Rose, J.J., Wang, L., Xu, Q., McTiernan, C.F., Shiva, S., Tejero, J., & Gladwin, M.T. (2017). Carbon Monoxide Poisoning: Pathogenesis, Management, and Future Directions of Therapy. Am J Respir Crit Care Med, 195(5), 596-606.American Thoracic Society. doi: 10.1164/rccm.201606-1275CI.
Azarov, I., Wang, L., Rose, J.J., Xu, Q., Huang, X.N., Belanger, A., Wang, Y., Guo, L., Liu, C., Ucer, K.B., McTiernan, C.F., O'Donnell, C.P., Shiva, S., Tejero, J., Kim-Shapiro, D.B., & Gladwin, M.T. (2016). Five-coordinate H64Q neuroglobin as a ligand-trap antidote for carbon monoxide poisoning. Sci Transl Med, 8(368), 368ra173.American Association for the Advancement of Science (AAAS). doi: 10.1126/scitranslmed.aah6571.
Corti, P., Ieraci, M., & Tejero, J. (2016). Characterization of zebrafish neuroglobin and cytoglobins 1 and 2: Zebrafish cytoglobins provide insights into the transition from six-coordinate to five-coordinate globins. Nitric Oxide, 53, 22-34.Elsevier. doi: 10.1016/j.niox.2015.12.004.
Corti, P., Xue, J., Tejero, J., Wajih, N., Sun, M., Stolz, D.B., Tsang, M., Kim-Shapiro, D.B., & Gladwin, M.T. (2016). Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells. Proc Natl Acad Sci U S A, 113(30), 8538-8543.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.1522670113.
Tejero, J., Kapralov, A.A., Baumgartner, M.P., Sparacino-Watkins, C.E., Anthonymutu, T.S., Vlasova, I.I., Camacho, C.J., Gladwin, M.T., Bayir, H., & Kagan, V.E. (2016). Peroxidase activation of cytoglobin by anionic phospholipids: Mechanisms and consequences. Biochim Biophys Acta, 1861(5), 391-401.Elsevier. doi: 10.1016/j.bbalip.2016.02.022.
Singamsetty, S., Watanabe, Y., Guo, L., Corey, C., Wang, Y., Tejero, J., McVerry, B.J., Gladwin, M.T., Shiva, S., & O'Donnell, C.P. (2015). Inorganic nitrite improves components of the metabolic syndrome independent of weight change in a murine model of obesity and insulin resistance. J Physiol, 593(14), 3135-3145.Wiley. doi: 10.1113/JP270386.
Tejero, J., Sparacino-Watkins, C.E., Ragireddy, V., Frizzell, S., & Gladwin, M.T. (2015). Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket. Biochemistry, 54(3), 722-733.American Chemical Society (ACS). doi: 10.1021/bi501196k.
Wang, J., Krizowski, S., Fischer-Schrader, K., Niks, D., Tejero, J., Sparacino-Watkins, C., Wang, L., Ragireddy, V., Frizzell, S., Kelley, E.E., Zhang, Y., Basu, P., Hille, R., Schwarz, G., & Gladwin, M.T. (2015). Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide. Antioxid Redox Signal, 23(4), 283-294.Mary Ann Liebert. doi: 10.1089/ars.2013.5397.
Haque, M.M., Bayachou, M., Tejero, J., Kenney, C.T., Pearl, N.M., Im, S.C., Waskell, L., & Stuehr, D.J. (2014). Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles. FEBS J, 281(23), 5325-5340.Wiley. doi: 10.1111/febs.13073.
Ramasamy, S., Haque, M.M., Tejero, J., Gangoda, M., & Stuehr, D. (2014). Probing the mechanism of tetrahydrobiopterin radical reduction within NO synthases. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 42, 138-139.Elsevier. doi: 10.1016/j.niox.2014.09.118.
Sparacino-Watkins, C., Ragireddy, V., Gladwin, M., & Tejero, J. (2014). Modulation of cytoglobin nitrite reductase rates by distal histidine mutations. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 42, 141.Elsevier. doi: 10.1016/j.niox.2014.09.125.
Sparacino-Watkins, C.E., Tejero, J., Sun, B., Gauthier, M.C., Thomas, J., Ragireddy, V., Merchant, B.A., Wang, J., Azarov, I., Basu, P., & Gladwin, M.T. (2014). Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. J Biol Chem, 289(15), 10345-10358.Elsevier. doi: 10.1074/jbc.M114.555177.
Tejero, J., & Gladwin, M.T. (2014). The globin superfamily: functions in nitric oxide formation and decay. Biol Chem, 395(6), 631-639.De Gruyter. doi: 10.1515/hsz-2013-0289.
Corti, P., Tejero, J., & Gladwin, M.T. (2013). Evidence mounts that red cells and deoxyhemoglobin can reduce nitrite to bioactive NO to mediate intravascular endocrine NO signaling: commentary on "Anti-platelet effects of dietary nitrate in healthy volunteers: involvement of cGMP and influence of sex". Free Radic Biol Med, 65, 1518-1520.Elsevier. doi: 10.1016/j.freeradbiomed.2013.09.020.
Haque, M.M., Tejero, J., Bayachou, M., Wang, Z.Q., Fadlalla, M., & Stuehr, D.J. (2013). Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis. FEBS J, 280(18), 4439-4453.Wiley. doi: 10.1111/febs.12404.
Raat, N.J.H., Tabima, D.M., Specht, P.A.C., Tejero, J., Champion, H.C., Kim-Shapiro, D.B., Baust, J., Mik, E.G., Hildesheim, M., Stasch, J.P., Becker, E.M., Truebel, H., & Gladwin, M.T. (2013). Direct sGC activation bypasses NO scavenging reactions of intravascular free oxy-hemoglobin and limits vasoconstriction. Antioxid Redox Signal, 19(18), 2232-2243.Mary Ann Liebert. doi: 10.1089/ars.2013.5181.
Sparacino-Watkins, C., Tejero, J., Wang, J., Ragireddy, V.P., Gauthier, M., Thomas, J., Bueno, M., Azarov, I., Lai, Y.C., Sun, B., Frizzell, S., Basu, P., Mora, A., & Gladwin, M.T. (2013). Novel human mitochondrial enzyme can transform nitrite into nitric oxide. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 31, S45-S46.Elsevier. doi: 10.1016/j.niox.2013.02.076.
Tejero, J., & Stuehr, D. (2013). Tetrahydrobiopterin in nitric oxide synthase. IUBMB Life, 65(4), 358-365.Wiley. doi: 10.1002/iub.1136.
Zhao, X.J., Wang, L., Shiva, S., Tejero, J., Myerburg, M.M., Wang, J., Frizzell, S., & Gladwin, M.T. (2013). Mechanisms for cellular NO oxidation and nitrite formation in lung epithelial cells. Free Radic Biol Med, 61, 428-437.Elsevier. doi: 10.1016/j.freeradbiomed.2013.04.031.
Tejero, J., Basu, S., Helms, C., Hogg, N., King, S.B., Kim-Shapiro, D.B., & Gladwin, M.T. (2012). Low NO concentration dependence of reductive nitrosylation reaction of hemoglobin. J Biol Chem, 287(22), 18262-18274.Elsevier. doi: 10.1074/jbc.M111.298927.
Tiso, M., Tejero, J., Kenney, C., Frizzell, S., & Gladwin, M.T. (2012). Nitrite reductase activity of nonsymbiotic hemoglobins from Arabidopsis thaliana. Biochemistry, 51(26), 5285-5292.American Chemical Society (ACS). doi: 10.1021/bi300570v.
Wang, Z.Q., Tejero, J., Wei, C.C., Haque, M.M., Santolini, J., Fadlalla, M., Biswas, A., & Stuehr, D.J. (2012). Arg375 tunes tetrahydrobiopterin functions and modulates catalysis by inducible nitric oxide synthase. J Inorg Biochem, 108, 203-215.Elsevier. doi: 10.1016/j.jinorgbio.2011.11.015.
Donadee, C., Raat, N.J.H., Kanias, T., Tejero, J., Lee, J.S., Kelley, E.E., Zhao, X., Liu, C., Reynolds, H., Azarov, I., Frizzell, S., Meyer, E.M., Donnenberg, A.D., Qu, L., Triulzi, D., Kim-Shapiro, D.B., & Gladwin, M.T. (2011). Nitric oxide scavenging by red blood cell microparticles and cell-free hemoglobin as a mechanism for the red cell storage lesion. Circulation, 124(4), 465-476.Wolters Kluwer. doi: 10.1161/CIRCULATIONAHA.110.008698.
Gladwin, M.T., & Tejero, J. (2011). Nitrite-NO bailout for a NOS complex too big to fail. Nat Med, 17(12), 1556-1557.Springer Nature. doi: 10.1038/nm.2591.
Hannibal, L., Somasundaram, R., Tejero, J., Wilson, A., & Stuehr, D.J. (2011). Influence of heme-thiolate in shaping the catalytic properties of a bacterial nitric-oxide synthase. J Biol Chem, 286(45), 39224-39235.Elsevier. doi: 10.1074/jbc.M111.286351.
Haque, M.M., Kenney, C., Tejero, J., & Stuehr, D.J. (2011). A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains. FEBS J, 278(21), 4055-4069.Wiley. doi: 10.1111/j.1742-4658.2011.08310.x.
Jayaraman, T., Tejero, J., Chen, B.B., Blood, A.B., Frizzell, S., Shapiro, C., Tiso, M., Hood, B.L., Wang, X., Zhao, X., Conrads, T.P., Mallampalli, R.K., & Gladwin, M.T. (2011). 14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide. J Biol Chem, 286(49), 42679-42689.Elsevier. doi: 10.1074/jbc.M111.271973.
Tejero, J., Biswas, A., Haque, M.M., Wang, Z.Q., Hemann, C., Varnado, C.L., Novince, Z., Hille, R., Goodwin, D.C., & Stuehr, D.J. (2011). Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase. Biochem J, 433(1), 163-174.Portland Press. doi: 10.1042/BJ20101353.
Tiso, M., Kenney, C., Tejero, J., & Gladwin, M. (2011). Deoxygenated non-symbiotic plant hemoglobins function as nitrite reductases. NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 24, S25.Elsevier. doi: 10.1016/j.niox.2011.03.256.
Tiso, M., Tejero, J., Basu, S., Azarov, I., Wang, X., Simplaceanu, V., Frizzell, S., Jayaraman, T., Geary, L., Shapiro, C., Ho, C., Shiva, S., Kim-Shapiro, D.B., & Gladwin, M.T. (2011). Human neuroglobin functions as a redox-regulated nitrite reductase. J Biol Chem, 286(20), 18277-18289.Elsevier. doi: 10.1074/jbc.M110.159541.
Tejero, J., Hannibal, L., Mustovich, A., & Stuehr, D.J. (2010). Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J Biol Chem, 285(35), 27232-27240.Elsevier. doi: 10.1074/jbc.M110.138842.
Tejero, J., Haque, M.M., Durra, D., & Stuehr, D.J. (2010). A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. J Biol Chem, 285(34), 25941-25949.Elsevier. doi: 10.1074/jbc.M110.126797.
Ilagan, R.P., Tejero, J., Aulak, K.S., Ray, S.S., Hemann, C., Wang, Z.Q., Gangoda, M., Zweier, J.L., & Stuehr, D.J. (2009). Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase. Biochemistry, 48(18), 3864-3876.American Chemical Society (ACS). doi: 10.1021/bi8021087.
Stuehr, D.J., Tejero, J., & Haque, M.M. (2009). Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain. FEBS J, 276(15), 3959-3974.Wiley. doi: 10.1111/j.1742-4658.2009.07120.x.
Tejero, J., Santolini, J., & Stuehr, D.J. (2009). Fast ferrous heme-NO oxidation in nitric oxide synthases. FEBS J, 276(16), 4505-4514.Wiley. doi: 10.1111/j.1742-4658.2009.07157.x.
Tejero, J., Biswas, A., Wang, Z.Q., Page, R.C., Haque, M.M., Hemann, C., Zweier, J.L., Misra, S., & Stuehr, D.J. (2008). Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase. J Biol Chem, 283(48), 33498-33507.Elsevier. doi: 10.1074/jbc.M806122200.
Wei, C.C., Wang, Z.Q., Tejero, J., Yang, Y.P., Hemann, C., Hille, R., & Stuehr, D.J. (2008). Catalytic reduction of a tetrahydrobiopterin radical within nitric-oxide synthase. J Biol Chem, 283(17), 11734-11742.Elsevier. doi: 10.1074/jbc.M709250200.
Erzurum, S.C., Ghosh, S., Janocha, A.J., Xu, W., Bauer, S., Bryan, N.S., Tejero, J., Hemann, C., Hille, R., Stuehr, D.J., Feelisch, M., & Beall, C.M. (2007). Higher blood flow and circulating NO products offset high-altitude hypoxia among Tibetans. Proc Natl Acad Sci U S A, 104(45), 17593-17598.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.0707462104.
Haque, M.M., Panda, K., Tejero, J., Aulak, K.S., Fadlalla, M.A., Mustovich, A.T., & Stuehr, D.J. (2007). A connecting hinge represses the activity of endothelial nitric oxide synthase. Proc Natl Acad Sci U S A, 104(22), 9254-9259.Proceedings of the National Academy of Sciences. doi: 10.1073/pnas.0700332104.
Ray, S.S., Tejero, J., Wang, Z.Q., Dutta, T., Bhattacharjee, A., Regulski, M., Tully, T., Ghosh, S., & Stuehr, D.J. (2007). Oxygenase domain of Drosophila melanogaster nitric oxide synthase: unique kinetic parameters enable a more efficient NO release. Biochemistry, 46(42), 11857-11864.American Chemical Society (ACS). doi: 10.1021/bi700803p.
Tejero, J., Peregrina, J.R., Martínez-Júlvez, M., Gutiérrez, A., Gómez-Moreno, C., Scrutton, N.S., & Medina, M. (2007). Catalytic mechanism of hydride transfer between NADP+/H and ferredoxin-NADP+ reductase from Anabaena PCC 7119. Arch Biochem Biophys, 459(1), 79-90.Elsevier. doi: 10.1016/j.abb.2006.10.023.
Tiso, M., Tejero, J., Panda, K., Aulak, K.S., & Stuehr, D.J. (2007). Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail. Biochemistry, 46(50), 14418-14428.American Chemical Society (ACS). doi: 10.1021/bi701646k.
Sánchez, I.E., Tejero, J., Gómez-Moreno, C., Medina, M., & Serrano, L. (2006). Point mutations in protein globular domains: contributions from function, stability and misfolding. J Mol Biol, 363(2), 422-432.Elsevier. doi: 10.1016/j.jmb.2006.08.020.
Martínez-Júlvez, M., Tejero, J., Peregrina, J.R., Nogués, I., Frago, S., Gómez-Moreno, C., & Medina, M. (2005). Towards a new interaction enzyme:coenzyme. Biophys Chem, 115(2-3), 219-224.Elsevier. doi: 10.1016/j.bpc.2004.12.034.
Tejero, J., Pérez-Dorado, I., Maya, C., Martínez-Júlvez, M., Sanz-Aparicio, J., Gómez-Moreno, C., Hermoso, J.A., & Medina, M. (2005). C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H. Biochemistry, 44(41), 13477-13490.American Chemical Society (ACS). doi: 10.1021/bi051278c.
Nogués, I., Tejero, J., Hurley, J.K., Paladini, D., Frago, S., Tollin, G., Mayhew, S.G., Gómez-Moreno, C., Ceccarelli, E.A., Carrillo, N., & Medina, M. (2004). Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin. Biochemistry, 43(20), 6127-6137.American Chemical Society (ACS). doi: 10.1021/bi049858h.
Tejero, J., Martínez-Julvez, M., Mayoral, T., Luquita, A., Sanz-Aparicio, J., Hermoso, J.A., Hurley, J.K., Tollin, G., Gómez-Moreno, C., & Medina, M. (2003). Involvement of the pyrophosphate and the 2'-phosphate binding regions of ferredoxin-NADP+ reductase in coenzyme specificity. J Biol Chem, 278(49), 49203-49214.Elsevier. doi: 10.1074/jbc.M307934200.
Medina, M., Luquita, A., Tejero, J., Hermoso, J., Mayoral, T., Sanz-Aparicio, J., Grever, K., & Gomez-Moreno, C. (2001). Probing the determinants of coenzyme specificity in ferredoxin-NADP+ reductase by site-directed mutagenesis. J Biol Chem, 276(15), 11902-11912.Elsevier. doi: 10.1074/jbc.M009287200.
Gladwin, M., DeMartino, A., Poudel, L., Dent, M., Chen, X., Xu, Q., Gladwin, B., Tejero, J., Basu, S., Alipour, E., Jiang, Y., Rose, J., & Shapiro, D. (2024). Formation and signaling by an NO-ferroheme complex provides a novel pathway for intravascular and intracellular NO signaling. In Formation and signaling by an NO-ferroheme complex provides a novel pathway for intravascular and intracellular NO signaling.ScienceOpen. doi: 10.14293/cgmp.24000052.v1.
Amdahl, M.B., Corti, P., Sparacino-Watkins, C., Tejero, J., Straub, A., & Gladwin, M. (2014). Reduction of Hexacoordinate Globins by Cytochrome B5. In FREE RADICAL BIOLOGY AND MEDICINE, 76, (p. S138).Elsevier. doi: 10.1016/j.freeradbiomed.2014.10.105.
Azarov, I., Wang, L., Huang, N., Belanger, A., Liu, C., O'Donnell, C., Shiva, S., Tejero, J., Kim-Shapiro, D., & Gladwin, M. (2014). Antidote for carbon monoxide poisoning. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 42, (pp. 100-101).Elsevier. doi: 10.1016/j.niox.2014.09.011.
Azarov, I., Wang, L., McTiernan, C., Belanger, A., Zhi, C., Rose, J., Liu, C., Huang, N., Ragireddy, P., Shiva, S., Tejero, J., Kim-Shapiro, D., & Gladwin, M. (2014). Antidote for Carbon Monoxide Poisoning. In FREE RADICAL BIOLOGY AND MEDICINE, 76, (p. S78).Elsevier. doi: 10.1016/j.freeradbiomed.2014.10.278.
Corti, P., Ieraci, M., Gladwin, M., & Tejero, J. (2014). Reduction of nitrite to NO by zebrafish (Danio rerio) six-coordinate heme globins. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 42, (pp. 118-119).Elsevier. doi: 10.1016/j.niox.2014.09.060.
Wang, J., Krizowski, S., Fischer, K., Niks, D., Tejero, J., Sparacino-Watkins, C., Wang, L., Ragireddy, V., Frizzell, S., Kelley, E., Zhang, Y., Basu, P., Hille, R., Schwarz, G., & Gladwin, M. (2014). Sulfite oxidase catalyzes single electron transfer at molybdenum domain to reduce nitrite to nitric oxide. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 42, (p. 149).Elsevier. doi: 10.1016/j.niox.2014.09.146.
Corti, P., Tejero, J., Tsang, M., & Gladwin, M. (2013). Nitrite exposure under hypoxia improve heart regeneration in zebrafish. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 31, (pp. S31-S32).Elsevier. doi: 10.1016/j.niox.2013.02.044.
Tejero, J., Ragireddy, V., Azarov, I., Corti, P., Frizzell, S., & Gladwin, M. (2013). Effect of distal heme pocket mutations on neuroglobin nitrite reduction rates. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 31, (p. S23).Elsevier. doi: 10.1016/j.niox.2013.02.027.
Wang, J., Krizowski, S., Fischer, K., Niks, D., Tejero, J., Wang, L., Sparacino-Watkins, C., Ragireddy, P., Frizzell, S., Kelley, E.E., Shiva, S., Zhang, Y., Basu, P., Hille, R., Schwarz, G., & Gladwin, M.T. (2013). Sulfite oxidase catalyzes single electron transfer at molybdenum domain to reduce nitrite to NO. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 31, (pp. S39-S40).Elsevier. doi: 10.1016/j.niox.2013.02.064.
Tejero, J., Ragireddy, V., Azarov, I., Frizzell, S., & Gladwin, M.T. (2012). Changes in the Distal Heme Pocket of Neuroglobin Modulate Autoxidation Rates. In FREE RADICAL BIOLOGY AND MEDICINE, 53, (p. S152).Elsevier. doi: 10.1016/j.freeradbiomed.2012.10.415.
Corti, P., Tejero, J., & Gladwin, M.T. (2011). Purification and Characterization of Zebrafish (Danio Rerio) Globin X. In FREE RADICAL BIOLOGY AND MEDICINE, 51, (pp. S163-S164).Elsevier. doi: 10.1016/j.freeradbiomed.2011.10.231.
Donadee, C., Raat, N.J.H., Tejero, J., Lee, J.S., Kelley, E., Zhao, X., Liu, C., Reynolds, H., Azarov, I., Meyer, E.M., Donnenberg, A., Qu, L., Triulzi, D., Kim-Shapiro, D., & Gladwin, M.T. (2011). Nitric Oxide Scavenging By Red Cell Microparticles And Cell Free Hemoglobin As A Mechanism For The Red Cell Storage Lesion. In D35. OXIDANTS AND ANTIOXIDANTS, (p. a5955).American Thoracic Society. doi: 10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5955.
Tejero, J., Ragireddy, V., Azarov, I., Corti, P., Frizzell, S., & Gladwin, M.T. (2011). Exploring the Mechanism of Fast Nitrite Reduction by Five-Coordinate Neuroglobin. In FREE RADICAL BIOLOGY AND MEDICINE, 51, (p. S150).Elsevier. doi: 10.1016/j.freeradbiomed.2011.10.260.
Wang, J., Fischer, K., Krizowski, S., Tejero, J., Zhao, X., Wang, L., Frizzell, S., Schwarz, G., & Gladwin, M. (2011). Sulfite oxidase: A novel nitrite reductase that generates nitric oxide. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 24, (pp. S30-S31).Elsevier. doi: 10.1016/j.niox.2011.03.272.
Wang, J., Krizowski, S., Fischer, K., Tejero, J., Zhao, X., Wang, L., Frizzell, S., Kelley, E., Schwarz, G., & Gladwin, M.T. (2011). Sulfite Oxidase: a Novel Nitrite Reductase that Generates Nitric Oxide. In FREE RADICAL BIOLOGY AND MEDICINE, 51, (p. S164).Elsevier. doi: 10.1016/j.freeradbiomed.2011.10.233.
Zhao, X.J., Shiva, S., Tejero, J., Wang, L., Wang, J., Frizzell, S., & Gladwin, M. (2011). Mechanisms for cellular nitrite formation: Role of ceruloplasmin and oxygen. In NITRIC OXIDE-BIOLOGY AND CHEMISTRY, 24, (pp. S38-S39).Elsevier. doi: 10.1016/j.niox.2011.03.294.
Basu, S., Bravo, J.T., Reuter, B., King, S.B., Hogg, N., Gladwin, M.T., & Kim-Shapiro, D.B. (2010). Evidence for S-nitrosothiol Formation by a Nitrite Dependent Pathway During Reductive Nitrosylation of Ferric Hemoglobin. In FREE RADICAL BIOLOGY AND MEDICINE, 49, (p. S108).Elsevier. doi: 10.1016/j.freeradbiomed.2010.10.286.
Tejero, J., Basu, S., Carlisle, C., Hogg, N., King, S.B., Kim-Shapiro, D.B., & Gladwin, M.T. (2010). The Reductive Nitrosylation of Hemoglobin: Low Nitric Oxide Effects and Mechanisms for N2O3 Formation. In FREE RADICAL BIOLOGY AND MEDICINE, 49, (p. S121).Elsevier. doi: 10.1016/j.freeradbiomed.2010.10.332.
Tiso, M., Tejero, J., Basu, S., Azarov, I., Wang, X., Simplaceanu, V., Frizzell, S., Jayaraman, T., Geary, L., Shapiro, C., Ho, C., Shiva, S., Kim-Shapiro, D.B., & Gladwin, M.T. (2010). Heme Coordination and Nitrite Reductase Activity of Human Neuroglobin. In FREE RADICAL BIOLOGY AND MEDICINE, 49, (p. S121).Elsevier. doi: 10.1016/j.freeradbiomed.2010.10.331.
Wang, J., Fischer, K., Zhao, X., Tejero, J., Kelley, E.E., Wang, L., Shiva, S., Frizzell, S., Zhang, Y., Basu, P., Schwarz, G., & Gladwin, M.T. (2010). Novel Function of Sulfite Oxidase as a Nitrite Reductase that Generates Nitric Oxide. In FREE RADICAL BIOLOGY AND MEDICINE, 49, (p. S122).Elsevier. doi: 10.1016/j.freeradbiomed.2010.10.335.