Vascular Medicine Institute
University of Pittsburgh
BST E1240
200 Lothrop Street
Pittsburgh, PA 15261
Phone: 412-383-5853
Fax: 412-648-5980

Jesus Tejero Bravo, PhD


Jesus Tejero


Jesus Tejero, PhD

Assistant Professor of Medicine,
Division of Pulmonary, Allergy and Critical Care Medicine

E1228-5A BST
200 Lothrop Street
Pittsburgh, PA 15261

Phone: 412-624-2651
Email: jet68@pitt.edu

Gladwin Lab



Dr. Tejero received his degree in Organic Chemistry at the University of Zaragoza, Spain in 1998 and earned his PhD in Biochemistry at the University of Zaragoza in 2004 with the thesis “Redesign of the coenzyme specificity of the ferredoxin-NADP+ reductase from Anabaena PCC 7119” under Prof. Carlos Gómez-Moreno and Dr. Milagros Medina. He moved to the United States in 2005 as research fellow at the lab of Dr. Dennis Stuehr at the Cleveland Clinic, Lerner Research Institute. His work there focused on the structure and function of nitric oxide synthases. He joined Dr. Gladwin lab at the University of Pittsburgh Vascular Medicine Institute as a research associate in May, 2009. Dr Tejero is currently an Assistant Professor in the Department of Pulmonary, Allergy and Critical Care Medicine.

Research Interests

Dr. Tejero’s research is focused on the biology of heme proteins. His main research goals include: i) to understand and characterize the chemical and kinetic features of the reactions of nitrite with hemoglobin, myoglobin, cytoglobin and neuroglobin, ii) to elucidate the cytoprotective mechanisms of the six-coordinate globins neuroglobin and cytoglobin, and iii) the development of heme-based antidotes for carbon monoxide poisoning.

Nitrite–heme reactions. The nitrite-heme reactions are of growing interest because of its role in nitric oxide signaling pathways and can play a significant role in physiological and pathological situations. The ability of heme proteins to produce NO under hypoxia and anoxia can be instrumental to cell survival through the activation of soluble guanylate cyclase, and the inhibition of cytochrome c oxidase and other heme proteins.

Cytoprotective mechanisms of neuroglobin and cytoglobin. Neuroglobin and cytoglobin are two proteins with important, yet unclear roles in cellular protection. Our work is aimed to determine the functions of neuroglobin and cytoglobin that regulate cell survival. By understanding how neuroglobin and cytoglobin protect the cells, this work can help to develop therapies that harness the protective effect of these proteins.

Heme-based antidotes for CO poisoning. We have recently characterized a neuroglobin mutant with very high affinity towards CO. The use of this protein in a mouse model of lethal CO poisoning has shown a significant decrease in mortality. We are working on further development of neuroglobin mutants and other heme-based molecules for the treatment of CO poisoning.


Some characteristics of vertebrate globins.
From Hankeln, T. et al., (2005) Journal of Inorganic Biochemistry 99, 110-119.

Key Publications

Amdahl MB, Sparacino-Watkins CE, Corti P, Gladwin MT, Tejero J (2017) Efficient Reduction of Vertebrate Cytoglobins by the Cytochrome b5/Cytochrome b5 Reductase/NADH System. Biochemistry 56, 3993-4004.

Azarov I, Wang L, Rose JJ, Xu Q, Huang XN, Belanger A, Wang Y, Guo L, Liu C, Ucer KB, McTiernan CF, O'Donnell CP, Shiva S, Tejero J, Kim-Shapiro DB, Gladwin MT (2016) Five-coordinate H64Q neuroglobin as a ligand-trap antidote for carbon monoxide poisoning. Science translational medicine 8, 368ra173.

Corti P, Xue J, Tejero J, Wajih N, Sun M, Stolz DB, Tsang M, Kim-Shapiro DB, & Gladwin MT. (2016) Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells. Proc Natl Acad Sci USA 113, 8538-8543.

Tejero J, Kapralov AA, Baumgartner MP, Sparacino-Watkins CE, Anthonymuthu TS. Vlasova II, Camacho CJ, Gladwin MT, Bayir H & Kagan VE. (2016) Peroxidase Activation of Cytoglobin by Anionic phospholipids: Mechanisms and Consequences. BBA-Mol. Cell Biol. L. 1861, 391-401.

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.

Tejero J, Sparacino-Watkins CE, Ragireddy V, Frizzell S & Gladwin MT. (2015) Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket. Biochemistry 54, 722-733.

Sparacino-Watkins CE, Tejero J, Gauthier MC, Ragireddy V, Thomas J, Azarov I, Wang J, Merchant B, Basu P & Gladwin MT. (2014) Nitrite reductase and NO synthase activity of the mitochondrial molybdopterin enzymes mARC (MOSC) 1 and 2. J. Biol. Chem. 289, 10345-10358.

Tejero J, Basu S, Helms C, Hogg N, King SB, Kim-Shapiro DB & Gladwin MT. (2012) Low NO concentration-dependence of the reductive nitrosylation reaction of haemoglobin. J. Biol. Chem. 287, 18262-18274.

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 DB & Gladwin MT. (2011) Human neuroglobin functions as a redox regulated nitrite reductase. J. Biol. Chem. 286, 18277-18289.

Tejero J, Hannibal L, Mustovich A & Stuehr DJ. (2010) Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J. Biol. Chem., 285, 27232-27240.

Tejero J, Biswas A, Wang ZQ, Page RC, Haque MM, Hemann C, Zweier JL, Misra S and Stuehr DJ. Stabilization and characterization of a heme-oxy reaction intermediate in inducible nitric-oxide synthase. J Biol Chem. 283: 33498-33507, 2008.

Tejero J, Pérez-Dorado I, Maya C, Martínez-Júlvez M, Sanz-Aparicio J, Gómez-Moreno C, Hermoso JA, Medina M. C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H. Biochemistry 44:13477-13490, 2005.

Tejero J, Martínez-Julvez M, Mayoral T, Luquita A, Sanz-Aparicio J, Hermoso JA, Hurley JK, Tollin G, Gómez-Moreno C, Medina M. Involvement of the pyrophosphate and the 2'-phosphate binding regions of ferredoxin-NADP+ reductase in coenzyme specificity. J Biol Chem. 278:49203-49214, 2003.

Pubmed link