Areas of Interest
Research Foci: Chemical biology of hydrogen sulfide signaling, regulation of mammalian sulfur metabolism in health and disease, structural enzymology of human B12 trafficking proteins.
Toxic at high concentrations, H2S is a signaling molecule produced by cells and modulates important physiological processes including blood pressure regulation, inflammation and neuoromodulation. Our laboratory is investigating the reaction mechanisms and regulation of enzymes involved in H2S biogenesis and its clearance via oxidation. In addition to the canonical mitochondrial sulfide oxidation pathway, we have recently discovered a new pathway for clearing H2S, which involves hemeproteins. We use a combination of spectroscopic (EPR, fluorescence), kinetic (stopped-flow spectroscopy) and cellular approaches to understand the mechanisms of catalysis and regulation of key enzymes involved in H2S homeostasis. The enzymes involved in sulfur metabolism are richly dependent on multiple B vitamins for their catalytic functions including vitamin B6, folic acid and B12. My laboratory is also studying the intricate network of chaperones that shepherd and tailor vitamin B12 from its point of entry into cells to its target enzymes and whose dysfunction lead to disease. We have been elucidating novel enzymatic functions of the individual proteins and the thermodynamics and kinetics of protein-protein interactions in the pathway that guide B12 delivery without dilution into the cellular milieu. Using a combination of structural, spectroscopic and kinetic approaches we are studying allosteric regulation in the trafficking pathway for cofactor delivery with high fidelity.
Honors & Awards
Merck Award, ASBMB, 2019
Associate Editor, Chemical Reviews, 2012–present
Associate Editor, Journal of Biological Chemistry, 2012–present
Elected Fellow, American Association for the Advancement of Science, 2011
Associate Chair, Department of Biological Chemistry, 2008–2019
Pfizer Award, American Chemical Society, 2001
Established Investigator, American Heart Association, 2000
Hydrogen sulfide stimulates lipid biogenesis from glutamine that is dependent on the mitochondrial NAD(P)H pool.
Carballal S, Vitvitsky V, Kumar R, Hanna DA, Libiad M, Gupta A, Jones JW, Banerjee R.
J Biol Chem. 2021; 297: 100950.
Protein aggregating ability of different protoporphyrin-IX nanostructures is dependent on their oxidation and protein binding capacity.
Maitra D, Pinsky BM, Soherawardy A, Zheng H, Banerjee R, Omary MB.
J Biol Chem. 2021; 297: 100778.
The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis.
Vitvitsky V, Kumar R, Libiad M, Maebius A, Landry A, Banerjee R.
J Biol Chem. 2021; 296: 100736.
HIF-2α activation potentiates oxidative cell death in colorectal cancers by increasing cellular iron.
Singhal R, Mitta SR, Das NK, Kerk SA, Sajjakulnukit P, Solanki S, Andren A, Kumar R, Olive KP, Banerjee R, Lyssiotis CA, Shah YM.
J Clin Invest. 2021; 131: e143691.
Mobile loop dynamics in adenosyltransferase control binding and reactivity of coenzyme B12.
Mascarenhas R, Ruetz M, McDevitt L, Koutmos M, Banerjee R.
Proc Natl Acad Sci U S A. 2020; 117: 30412–22.
Chlorocob(II)alamin Formation Which Enhances the Thiol Oxidase Activity of the B12-Trafficking Protein CblC.
Li Z, Greenhalgh ED, Twahir UT, Kallon A, Ruetz M, Warncke K, Brunold TC, Banerjee R.
Inorg Chem. 2020; 59: 16065–72.
Dismantling and Rebuilding the Trisulfide Cofactor Demonstrates Its Essential Role in Human Sulfide Quinone Oxidoreductase.
Landry AP, Moon S, Bonanata J, Cho US, Coitiño EL, Banerjee R.
J Am Chem Soc. 2020; 142: 14295–306.
Structural perspectives on H2S homeostasis.
Landry AP, Roman J, Banerjee R.
Curr Opin Struct Biol. 2021; 71: 27–35.
Redox-Linked Coordination Chemistry Directs Vitamin B12 Trafficking.
Banerjee R, Gouda H, Pillay S.
Acc Chem Res. 2021; 54: 2003–13.
Regulation of the redox metabolome and thiol proteome by hydrogen sulfide.
Kumar R, Banerjee R.
Crit Rev Biochem Mol Biol. 2021; 56: 221–35.
For a list of publications from PubMed, click HERE