Blanca L. Barquera

Blanca L. Barquera

Bacteria are the most abundant organisms on earth. They are found almost every possible biological niche, from ordinary soil to deep oceans and geological formations. They also interact with the human body; some bacteria are essential for life while others can be deadly. The ability of bacteria to flourish in such a wide range of environments is due in large part to the enzymes that populate their cell membranes. These enzymes make up the active interface between the cell and the environment. One of their roles is to ensure the interior of the cell is a hospitable place for the biochemistry of life in spite of changing and often hostile conditions outside. 

Among the most important of these membrane enzymes are the ones that transport ions into and out of the cell. These ion transporters are essential for maintaining favorable concentrations of ions inside the cell but ion transport is also at the heart of energy production in the cell. Transport of H+ and Na+ create gradients that provide energy for processes as diverse as motility of the cell, import of nutrients and extrusion of chemicals that are toxic to the cell--the latter is responsible for an important class of antibiotic resistance. 

Our goal is to understand the mechanisms of the enzymes that enable bacteria to create and utilize these ion gradients and to determine the roles played by both the enzymes and gradients in the physiology of the cells. This will provide fundamental insights into the ways that bacteria affect human health, both when they are beneficial and when they are harmful.  

The projects in my laboratory range from basic microbiology, characterizing the physiology of bacteria and their interactions with other cells, to biophysical chemistry, spectroscopy (visible, fluorescence, FTIR, and EPR) and rapid kinetics in order to understand the molecular mechanisms of ion transport and energy production enzymes. We study Vibrio cholerae, the cause of the disease cholera, Pseudomonas aeruginosa which are implicated in cystic fibrosis, as well as Bacteroides fragilis, which are beneficial gut bacteria, and use infection models including mice, macrophages, and fruit flies. 

We are particularly interested in two enzymes: Na+-pumping NADH:quinone oxidoreductase (NQR), a respiratory enzyme found only in bacteria that uniquely pumps Na+ instead of H+, and Na+ pumping Ferredoxin:NAD oxidoreductase (RNF). These enzymes, are found in many pathogens, marine bacteria, and colon bacteria and are important for adaptation and proliferation of these organisms in diverse environments. In the case of NQR, my group defined the redox cofactors of the enzyme, their redox reactions, the pathway of electron transfer through these cofactors, and which of these electron transfer steps are linked to energy conservation. We are currently trying to understand the pathway that carries Na+ across the membrane and the mechanism that couples the redox reactions to this uphill transport of Na+.  

  • B.S. Chemistry

    Ph.D.  Biochemistry National University of Mexico

    University of Illinois/University of Helsinki

     

  • Hazan R, Que YA, Maura D, Strobel B, Majcherczyk PA, Hopper LR, Wilbur DJ, Hreha TN, Barquera B, Rahme LG. Auto Poisoning of the Respiratory Chain by a Quorum-Sensing-Regulated Molecule Favors Biofilm Formation and Antibiotic Tolerance. Curr Biol. 2016 Jan 25;26(2):195-206. doi: 10.1016/j.cub.2015.11.056. Epub 2016 Jan 14. PMID: 26776731
  • Tuz K, Mezic KG, Xu T, Barquera B, Juarez O. 2015.The kinetic reaction mechanism of the Vibrio cholerae sodium -dependent NADH Dehydrogenase. J Biol Chem. 2015 May 23. pii: jbc.M115.658773. [Epub ahead of print] PMID: 26004776
  • Hreha TN, Mezic KG, Herce HD, Duffy EB, Bourges A, Pryshchep S, Juarez O, Barquera B.2015. Topology of the RNF Complex from Vibrio cholerae. Biochemistry. Apr 21;54(15):2443-55. doi: 10.1021/acs.biochem.5b00020. Epub 2015 Apr 10. PMID: 25831459
  • Shea ME, Mezic KG, Juárez O, Barquera B. 2015. A mutation in Na(+)-NQR uncouples electron flow from Na(+) translocation in the presence of K(+). Biochemistry. Jan 20;54(2):490-6. doi: 10.1021/bi501266e. Epub 2014 Dec 22. PMID: 25486106
  • Barquera B. 2014.The sodium pumping NADH:quinone oxidoreductase (Na(+)-NQR), a unique redox-driven ion pump. J Bioenerg Biomembr. 46:289-298. doi:10.1007/s10863-014-9565-9. Epub 2014 Jul 23. PubMed PMID: 25052842.
  • Strickland M, Juárez O, Neehaul Y, Cook DA, Barquera B, Hellwig P. 2014. The Conformational Changes Induced by Ubiquinone Binding in the Na+-pumping NADH:Ubiquinone Oxidoreductase (Na+-NQR) Are Kinetically Controlled by Conserved Glycines 140 and 141 of the NqrB Subunit. J Biol Chem.289:23723-23733. doi: 10.1074/jbc.M114.574640. Epub 2014 Jul 8. PubMed PMID: 25006248; PubMed Central PMCID: PMC4156058.
  • Reyes-Prieto A, Barquera B, Juárez O. 2014. Origin and evolution of the sodium-pumping NADH: ubiquinone oxidoreductase. PLoS One. 9(5):e96696. doi: 10.1371/journal.pone.0096696. eCollection 2014.PubMed PMID: 24809444; PubMedCentral PMCID: PMC4014512.
  • Shea ME, Juárez O, Cho J, Barquera B. Aspartic acid 397 in subunit B of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae forms part of a sodium-binding site, is involved in cation selectivity, and affects cation-binding site cooperativity. 2013. J Biol Chem. 288:31241-1249. doi:10.1074/jbc.M113.510776. Epub 2013 Sep 12. PubMed PMID: 24030824; PubMed Central PMCID: PMC3829434.
  • Neehaul Y, Juárez O, Barquera B, Hellwig P. Infrared spectroscopic evidence of a redox-dependent conformational change involving ion binding residue NqrB-D397 in the Na(+)-pumping NADH:quinone oxidoreductase from Vibrio cholerae. 2013.Biochemistry. 52:3085-30893. doi: 10.1021/bi4000386. Epub 2013 Apr24. PubMed PMID: 23566241.
  • Juárez O, Neehaul Y, Turk E, Chahboun N, DeMicco JM, Hellwig P, Barquera B.2012. The role of glycine residues 140 and 141 of subunit B in the functional ubiquinone binding site of the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae. J Biol Chem. 287:25678-85. doi:10.1074/jbc.M112.366088. Epub 2012 May 29. PubMed PMID: 22645140; PubMed Central PMCID: PMC3408181.