Madhavan Narayanan, PhD

Madhavan Narayanan, PhD

Assistant Professor

Phone: 630-829-6559
Office Location: Birck 330

BenU faculty since 2020
Ph.D. – Temple University, Philadelphia, PA
M.Sc. – Indian Institute of Technology Bombay, Mumbai, India
B.Sc. – University of Madras, Chennai, India

Courses Taught
Introduction to Chemistry, Biochemistry

PEER REVIEWED PUBLICATIONS IN THE DISCIPLINE

  1. Incubating the SENCER Ideals with Project-Based Learning and Undergraduate Research, R. D Sieg, N. Beverly, Madhavan Narayanan, G. Surendran, J. Sabatini, D. S. Smyth, Science Education and Civic Engagement-An International Journal, Volume 11 Issue 1 · Winter 2019
  1. Madhavan Narayanan, Vijay R. Singh, Goutham Kodali, Katarina Moravcevic, and Robert J. Stanley, (2017) An Ethenoadenine FAD Analog Accelerates UV Dimer Repair by DNA Photolyase. Photochemistry and photobiology, 93: 343–354
  1. Madhavan Narayanan, S. Leung, Y. Inaba, M. Elguindy, E. Nakamaru-Ogiso (2015) Semiquinone intermediates are involved in the energy coupling mechanism of E. coli. Complex I, Biochimica et Biophysica acta – Bioenergetics 1847, 8, 681–689
  1.  E. Nakamaru-Ogiso, Madhavan Narayanan, J. Sakyiama, (2014) Roles of semiquinone species in proton pumping mechanism by complex I, J. Bioenerg. Biomembr., 46(4):269-77
  1. Madhavan Narayanan, D. Gabrieli, S. Leung, M. Elguindy, C. Glaser, N. Saju, S. Sinha, E. Nakamaru- Ogiso, (2013) Semiquinone and Cluster N6 Signals in His-tagged Proton-translocating NADH:Ubiquinone Oxidoreductase (Complex I) from Escherichia coli. J. Biol. Chem. 288: 14310-14319
  1. Madhavan Narayanan, G. Kodali, V. Velvadapu, V. Singh, R. Stanley (2012) Oxidation and reduction potentials of 8-vinyladenosine measured by cyclic voltammetry: Implications for photoinduced electron transfer quenching of a fluorescent adenine analog, J. Photochem. Photobiology, 249, 9-14
  1. G. Kodali, Madhavan Narayanan, R. Stanley (2012) Excited-State Electronic Properties of 6-Methyl-isoxanthopterin (6-MI): An Experimental and Theoretical Study, J. Phys. Chem. B, 116, 2981-2989
  1. Madhavan, Narayanan, G. Kodali, V. Singh, Y. Xing, R. Stanley, (2010) Differential quenching of fluorescent base analogs by nucleotide monophosphates, J. Phys. Chem. B, 114 (17), pp 5953–5963)
  1. Madhavan Narayanan, G. Kodali, Y.Xing, and R.Stanley, (2010) Photoinduced electron transfer occurs between 2-aminopurine and the DNA nucleic acid monophosphates: results from cyclic voltammetry and fluorescence quenching, J. Phys. Chem. B, 114 (32), pp 10573–10580.
  1. G. Kodali, K. A. Kistler, Madhavan Narayanan, S. Matsika and R. Stanley, (2010) Change in electronic structure upon optical excitation of 8-Vinyladenosine: An Experimental and Theoretical Study. J. Phys. Chem. A, 114 (1), pp 256–267

BOOK CHAPTERS

  1. The Role of Adenine in the Initial Photoinduced Electron Transfer Repair of UV-Damaged DNA By DNA Photolyase, R. Stanley, V. Singh, K. Jacoby, Madhavan Narayanan, S. Munshi, K. Moravcevic, (2013) Flavins and Flavoproteins, 403-408
  2. Study of photoinduced electron transfer in Fluorescent Nucleic acid base analogs (FBAs) and DNA photolyase, by Madhavan Narayanan, Ph.D., (2011) Temple University, 224 pages, ProQuest, UMI Dissertation Publishing, ISBN-13: 978-1-124-46575-3
  3. Intermediates in the ultrafast repair of DNA by DNA photolyase. Z. Hou, G. Kodali, Madhavan Narayanan, K. Yang, R. J. Stanley (2006) Femtochemistry VII: Fundamental Ultrafast Processes in Chemistry, Physics, and Biology, Pages 337–345, Edited by: A. Welford Castleman, Jr. and Michele L. Kimble ISBN: 978-0-444-52821-6
Research:

Research Area
Biochemistry, biophysical chemistry, computational chemistry, chemical education

Dr. Narayanan research focuses on the computational and experimental approaches to studying structure and dynamics of biomolecules. More specifically he is interested in developing and characterizing new fluorescent nucleic acid bases (FBAs), understanding the mechanism of mitochondrial electron transport chain protein called Complex I, purification and characterize-ation of photolyases/crytochromes in various species.

Summer Research:

Madhavan Narayanan, Ph.D.
Assistant Professor, Physical Sciences
[email protected]

Research Area
Biochemistry, biophysical chemistry, computational chemistry, chemical education

Research
Project 1: S-Adenosyl methionine (SAM) synthetase is an enzyme that binds to ATP and the amino acid methionine as substrates and converts them into S-Adenosyl Methionine. We would like to test if fluorescent nucleotide triphosphate analogs of adenine can serve as substrates for SAM-synthetase. If the enzyme can accept the modified fluorescent substrate, we can produce fluorescent analogs of S-adenosyl methionine. In this project, the student will design the gene to express and purify the protein. Once purified, the protein will be tested for its activity with natural and modified substrate.

Project 2: Flavoenzymes are proteins that contain flavin adenine dinuclueotide (FAD, an organic molecule) or other flavin derivatives as coenzymes and catalyze the conversion of a specific substrate (a reactant) into a product. DNA photolyase is a flavoenzyme which typically contains FAD as the catalytic cofactor and in the presence of blue-light catalyzes the repair of UV-damaged DNA. In this project, we will use molecular biology techniques to engineer a plasmid necessary for expressing the protein DNA photolyase from planaria in E. coli. Once the plasmid is engineered, we will work on expressing, purifying and characterizing the protein.

Project 3: The Tiny Earth initiative project is a part of the Microbiology Lab (Biol 3208) which involves crowdsourcing to find antibiotics in soil bacterial samples. In this project students at various institutions collect soil from their own selected location and isolate bacteria from the soil. The bacteria are then tested against safe relative bacteria of known pathogenic antibiotic-resistance to determine if the isolated bacteria are antibiotic-producers. The project often stops at this stage, as is the case with BenU. However, some Universities and colleges go on to have the structure of the antibiotic determined and/or identified. Dr. Poch and I would like to pilot through the NSSRP, the extraction and identification of the structure of antibiotics at BenU. Dr. Poch has curated at least 20 antibiotic-producing bacteria that can be used for extraction, purification and identification of the new antibiotics. The antibiotic compound(s) that are extracted from these bacteria will be separated using High Performance Liquid Chromatography (HPLC) and tested to determine which of the separated compounds has the antibiotic activity. Once sufficient quantity of the antibiotic is produced, their structure could be determined through NMR spectroscopy.