The University of Massachusetts Amherst

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Michael Maroney


Research in my group involves using biophysical, molecular biological and synthetic model approaches to elucidate the structure of transition metal sites in proteins and enzymes, and investigate how these sites function in biology.

Current Research
We have focused our efforts on nickel biochemistry and redox systems involving S-donor ligands. Systems that are of current interest in my group include proteins involved in nickel trafficking, and several enzymes including hydrogenase, superoxide dismutase and cysteine dioxygenase.

Learn more at

Academic Background

  • BS Iowa State University, 1977
  • PhD University of Washington, 1981
  • Postdoctoral Training: Northwestern University 1983, University Minnesota, 1983-1985
Y. Ha, H. Hu, K. Higgins, M. Maroney, B. Hedman, K. Hodgson, E. Solomon, “The Electronic Structure of the Metal Active Site Determines the Geometric Structure and Function of the Metalloregulator NikR,” Biochemistry, 2019,
B. S. Benavides, R. Acharya, E. R. Clark, P. Basak, M. J. Maroney, J. M. Nocek, K. S. Schanze, and D. M. Kurtz, “Structural, Photophysical, and Photochemical Characterization of Zinc Protoporphyrin IX in a Dimeric Variant of an Iron Storage Protein: Insights into the Mechanism of Photosensitized H2 Generation,” J. Phys. Chem. B, 2019, DOI: 10.1021/acs.jpcb.9b04817
H-T. Huang and M. J. Maroney, "Ni(II) Sensing by RcnR Does Not Require an FrmR-Like Inter-Subunit Linkage," Inorganic Chemistry, 2019,
H-T. Huang, S. Dillon, K. C. Ryan, J. O. Campecino, O. E. Watkins, D. E. Cabelli, T. C. Brunold, and M. J. Maroney, “The Role of Mixed Amine/Amide Ligation in Nickel Superoxide Dismutase, Inorg. Chem. 2018, 57,12521–12535.
C. A. E. M. Spronk, S. Żerko, M. Górka, W. Koźmiński, B. Bardiaux, B. Zambelli, F. Musiani, M. Piccioli, P. Basak, F. C. Blum, R. C. Johnson, H. Hu, D. S. Merrell, M. Maroney, S. Ciurli, “Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools, J. Biol. Inorg. Chem. 2018, 23, 1309 – 1330\. PubMed PMID: 30264175
V. D. Chaplin, J. A. Hangasky, H-T. Huang, R. Duan, M. J. Maroney, and M. J. Knapp, “Chloride Supports O2 Activation in the D201G Facial Triad Variant of FIH, an αKG Dependent Oxygenase, Inorg. Chem. 2018, 57, 12588-12595. DOI: 10.1021/acs.inorgchem.8b01736; PubMed PMID: 30252455; NIHMSID 1025499
H. Q. Hu, H-T. Huang and M. J. Maroney, “The Helicobacter pylori HypA•UreE2 complex contains a novel high-affinity Ni(II) binding site,” Biochemistry 2018, 57, 2932 – 2942. DOI: 10.1021/acs.biochem.8b00127, NIHMSID: NIHMS989119; PMID: 29708738
M. J. Maroney and R. J. Hondal, “Selenium versus sulfur: reversibility of chemical reactions and resistance to permanent oxidation in proteins and nucleic acids,” Free Radical Biology and Medicine 2018, 127, 228–237., NIHMS ID: NIHMS957915
H-T. Huang, C. E. Bobst, J. S. Iwig, P. T. Chivers, I. A. Kaltashov and M. J. Maroney, “Binding of Co(II) and Ni(II) orders the N-terminus and induces changes in helix dynamics that reduce DNA affinity in Escherichia coli RcnR protein,” J. Biol. Chem. 2018, 293, 324 - 332. doi:10.1074/jbc.RA117.000398. PMCID: PMC5766909
Contact Info

Department of Chemistry
N373 Life Sciences Laboratory
240 Thatcher Way
Amherst, MA 01003-9292

(413) 545-4876