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
A redox cycle with complex II prioritizes sulfide quinone oxidoreductase dependent H2S oxidation.
Kumar R, Landry AP, Guha A, Vitvitsky V, Lee HJ, Seike K, Reddy P, Lyssiotis CA, Banerjee R.
J Biol Chem. 2022; 298: 101435.
Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions.
Gouda H, Mascarenhas R, Pillay S, Ruetz M, Koutmos M, Banerjee R.
J Biol Chem. 2021; 297: 101373.
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.
Gas regulation of complex II reversal via electron shunting to fumarate in the mammalian ETC.
Banerjee R, Kumar R.
Trends Biochem Sci. 2022; 47: 689-98.
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.
For a list of publications from PubMed, click HERE