Brandon Greene

Assistant Professor
Joint Appt: BMSE

Office Hours

Weds 11:00 -12:00 pm

Contact Phone


Office Location

CHEM 1142C


Biomedical Sciences; Biologically Inspired Chemistry & Physics; Energy, Catalysis & Green Chemistry; Structural Chemistry, Spectroscopy & Advanced Analysis; Inorganic & Organometallic; Physical Chemistry; Biochemistry & Biophysics.


Brandon received his B.S. in Chemistry at Washington State University in 2009 where he developed a profound interest in biochemistry and biophysics. He pursued a Ph.D. in Chemistry at Emory University studying abiotic-biotic interfaces for photocatalysis, the enzymatic mechanisms of hydrogenases, and proton-coupled electron transfer (PCET) dynamics at bioinorganic cofactors in the group of R. Brian Dyer. He then pursued postdoctoral studies at Harvard/Massachusetts Institute of Technology defining the targets of allosteric control and conformational gating that initiate long-range radical transfer during nucleotide metabolism by ribonucleotide reductase in the labs of Daniel G. Nocera (Harvard) and JoAnne Stubbe (MIT).


Organisms in all branches of the tree of life harness exotic cofactors, macromolecular dynamics, and elegant reaction design to enable chemical transformations that occur far from equilibrium. Research in the Greene lab seeks to elucidate how biomolecular non-equilibrium reaction control is achieved. We are specifically interested in oxidation/reduction (redox) reactions that occur at potentials outside the solvent “redox window” of water that are relevant to bioenergy, biogeochemistry, and human health. Discoveries in these areas are enabled by a dynamic team of investigators of diverse expertise and a synergistic approach involving traditional and cutting-edge methods in protein engineering, molecular biology, spectroscopy, electrochemistry, and biomolecular structural analysis.


Cáceres, J. C., Dolmatch, A., and Greene, B. L. The Mechanism of Inhibition of Pyruvate Formate Lyase by Methacrylate. In review.

Bailey, C. A. and Greene, B. L. A Fluorometric Assay for High-throughput Phosphite Quantitation in Biological and Environmental Matrices. Analyst 2023, 148, 3650-3658.

Cáceres, J. C., Bailey, C. A., Yokoyama, K., and Greene, B. L. Selenocysteine substitution in thiyl radical enzymes. Method. Enzymol. 2022, 662, 119−140.

Greene, B. L. Progress and opportunities in photochemical enzymology of oxidoreductases. ACS Catal. 2021, 11, 14635−14650.

Cui, C., Greene, B. L., Kang, G., Drennan, C. L., Stubbe, J., and Nocera, D. G. Gated Proton Release During Radical Transfer at the Subunit Interface of Ribonucleotide Reductase. J. Am. Chem. Soc. 2021, 143, 176−183.

Greene, B. L., Stubbe, J., and Nocera, D. G. Selenocysteine Substitution into a Class I Ribonucleotide Reductase. Biochemistry 2019, 58, 5074‒5084.

Greene, B. L., Stubbe, J., and Nocera, D. G. “Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase” J. Am. Chem. Soc. 2018, 140, 15744-15752.

Greene, B. L., Taguchi, A. T., Stubbe, J., and Nocera, D. G. “Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase” J. Am. Chem. Soc. 2017, 140, 16657-16665.

Greene, B. L., Vansuch, G. E., Chica, B. C., Adams, M. W. W., and Dyer, R. B. “Applications of Photogating and Time Resolved Spectroscopy to Mechanistic Studies of Hydrogenases” Acc. Chem. Res. 2017, 50, 2718-2726.

Greene, B. L., Schut, G. J., Adams, M. W. W., and Dyer, R. B. “Pre-Steady-State Kinetics of Catalytic Intermediates of a [FeFe]-Hydrogenase” ACS Catal. 2017, 7, 2145-2150.

Greene, B. L., Vansuch, G. E., Wu, C. H., Adams, M. W. W., and Dyer, R. B. “Glutamate Gated Proton-coupled Electron Transfer Activity in a [NiFe]-Hydrogenase” J. Am. Chem. Soc. 2016, 138, 13013-13021.

Greene, B. L., Wu, C. H., Vansuch, G. E., Adams, M. W. W., and Dyer, R. B. “Proton Inventory and Dynamics in the Nia-S to Nia-C Transition of a [NiFe]-Hydrogenase” Biochemistry 2016, 55, 1813-1825.

Greene, B. L., Wu, C. H., McTernan, P. M., Adams, M. W. W., and Dyer, R. B. “Proton-coupled Electron Transfer Dynamics in the Catalytic Mechanism of a [NiFe]-Hydrogenase” J. Am. Chem. Soc. 2015, 137, 4558-4566.

Greene, B. L., Joseph, C. A., Maroney, M. J., and Dyer, R. B. “Direct Evidence of Active-site Reduction and Photodriven Catalysis in Sensitized Hydrogenase Assemblies” J. Am. Chem. Soc. 2012, 134, 11108-11111.