Sean Elliott, PhD
Boston University College of Arts and Sciences
Dept of Chemistry

PhD, California Institute of Technology

Sean Elliott investigates the connection between biological electron transfer chemistry and function of redox active proteins and enzymes, by using direct electrochemistry and spectroscopy. He joined the Department of Chemistry in 2002, following an EMBO Post-doctoral Fellowship at the University of Oxford. A recipient of the Gitner and Templeton Awards within the College of Arts and Sciences, he was promoted to Associate Professor of Chemistry in 2008.

The Elliott Group investigates the interplay between biological systems and redox-active species (e.g., metal ions, organic radicals, disulfide bonds, reactive oxygen species). Our emphasis is on the kinetic and thermodynamic basis for catalytic redox chemistry, as well as the molecular impact of metal ions and reactive oxygen species upon cells.

Bioelectrochemistry of Complex Metalloenzymes – The Elliott Group uses electrochemical tools, amongst others, to characterize the catalytic chemistry of redox active enzymes that are involved in multiple electron transfer steps. In particular, we use the technique of protein film voltammetry [PFV] to observe the reduction potentials of redox-cofactors that are a part of the essential machinery of an enzyme. Our laboratory interrogates a wide range of proteins and enzymes using this technique, and questions we are interested in vary from project to project.

Mechanisms of peroxidase catalysis have been investigated recently by our group using PFV. The bacterial cytochrome c peroxidases contain two heme groups, one of which is a five-coordinate active site of low reduction potential, and the other is a six-coordinate heme that is of higher potential, which serves a role in intermolecular electron transfer. We have certainly interrogated the enzyme from Nitrosomonas europaea, and determined that electroactive films of “NeCcP” give an electrochemical response indicating catalysis mediated by a n=1 ET step that is a part of the catalytic cycle.

Bacterial (multiheme) cytochromes are investigated in the Elliott Group using PFV. These include complex enzymes, such as the siroheme–dependent sulfite reductase, as well as simple cyt c-551 analogs and the less-simple cyt c-554, a tetraheme cytochrome.

The Redox Chemistry of Flavo- and Disulfide-enzymes – Other projects in the lab use electrochemistry as a way to probe the redox chemistry of enzymes involved in oxidative stress response, such as thioredoxin, glutaredoxin and thioredoxin reductases. This proven challenging due to the latent poor electrochemistry of disulfides, and the potential instability of flavo-proteins. However, we have been able to investigate a wide range of proteins such as thioredoxins and thioredoxin reductases. Thioredoxins are ubiquitous proteins that are small (~12 kDa), utilizing a surface-exposed disulfide bond as their means of storing and transferring electrons. Reduced thioredoxin is generated by a Trx reductase.

Techniques & Resources:

Protein film voltammetry (PFV) – a direct electrochemical suite of methods, is used to study protein-bound redox cofactors, allowing for the interrogation of previously inaccessible catalytic information

Bioinorganic Spectroscopies – the group makes use of optical absorption, fluorescence, and electron paramagnetic resonance spectroscopies routinely in the CIC, to further characterize the electronic structure and protein dynamics of redox enzymes.

Proteomic techniques are used to assess the impact of redox-active species (such as transition metals and reactive oxygen species) within living systems to investigate metal-ion import, packaging, and co-factor synthesis.

Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family
01/01/2017 - 12/31/2020 (PI)
NIH/National Institute of General Medical Sciences

Redox Reactions of the AdoMet Radical Enzyme Superfamily
08/15/2016 - 06/30/2020 (PI)
NIH/National Institute of General Medical Sciences

Structure-function relationships in metalloenzymes with multiple redox-active centers
09/01/2016 - 08/31/2019 (PI)
University of Wisconsin System National Science Fdn

Tuning Directionality for CO2 Reduction in the Oxo-Acid: Ferredoxin Superfamily
09/01/2014 - 08/31/2019 (PI)
Department of Energy

Connections Between Redox Chemistry and Catalysis in Multiheme Peroxidases
09/01/2013 - 08/31/2017 (PI)
National Science Foundation

Functionalization of Unactivated SP2-Hybridized Carbon Atoms
07/01/2014 - 06/30/2017 (PI)
Pennsylvania State University NIH NIGMS

Redox Reactivity of Thiroredoxin Disulfide Bonds
08/01/2011 - 07/31/2016 (PI)
National Science Foundation

Probing the mechanism and diversity of multi-electron redox reactions in sulfite
09/01/2011 - 02/20/2015 (PI)
NIH/National Institute of General Medical Sciences

Photo-Induced CO2 Reduction Using Reverse TCA Cycle Enzymes
01/01/2013 - 12/31/2014 (PI)
Research Corporation for Science Advancement

07/01/2010 - 06/30/2013 (PI)
City College of New York DOD AFOSR

Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.

  1. Kleingardner JG, Levin BD, Zoppellaro G, Andersson KK, Elliott SJ, Bren KL. Influence of heme c attachment on heme conformation and potential. J Biol Inorg Chem. 2018 Aug 24. PMID: 30143872.
  2. Maiocco SJ, Walker LM, Elliott SJ. Determining Redox Potentials of the Iron-Sulfur Clusters of the AdoMet Radical Enzyme Superfamily. Methods Enzymol. 2018; 606:319-339. PMID: 30097097.
  3. Maiocco SJ, Arcinas AJ, Landgraf BJ, Lee KH, Booker SJ, Elliott SJ. Transformations of the FeS Clusters of the Methylthiotransferases MiaB and RimO, Detected by Direct Electrochemistry. Biochemistry. 2016 Oct 04; 55(39):5531-5536. PMID: 27598886.
  4. Dowling DP, Miles ZD, Köhrer C, Maiocco SJ, Elliott SJ, Bandarian V, Drennan CL. Molecular basis of cobalamin-dependent RNA modification. Nucleic Acids Res. 2016 Nov 16; 44(20):9965-9976. PMID: 27638883.
  5. Blaszczyk AJ, Silakov A, Zhang B, Maiocco SJ, Lanz ND, Kelly WL, Elliott SJ, Krebs C, Booker SJ. Spectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase. J Am Chem Soc. 2016 Mar 16; 138(10):3416-26. PMID: 26841310; DOI: 10.1021/jacs.5b12592;.
  6. Frato KE, Walsh KA, Elliott SJ. Functionally Distinct Bacterial Cytochrome c Peroxidases Proceed through a Common (Electro)catalytic Intermediate. Biochemistry. 2016 Jan 12; 55(1):125-32. PMID: 26575087; DOI: 10.1021/acs.biochem.5b01162;.
  7. Wei Y, Li B, Prakash D, Ferry JG, Elliott SJ, Stubbe J. A Ferredoxin Disulfide Reductase Delivers Electrons to the Methanosarcina barkeri Class III Ribonucleotide Reductase. Biochemistry. 2015 Dec 1; 54(47):7019-28. PMID: 26536144; PMCID: PMC4697749; DOI: 10.1021/acs.biochem.5b01092;.
  8. Maiocco SJ, Grove TL, Booker SJ, Elliott SJ. Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster. J Am Chem Soc. 2015 Jul 15; 137(27):8664-7. PMID: 26088836; DOI: 10.1021/jacs.5b03384;.
  9. Stein N, Love D, Judd ET, Elliott SJ, Bennett B, Pacheco AA. Correlations between the Electronic Properties of Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) and Its Structure: Effects of Heme Oxidation State and Active Site Ligation. Biochemistry. 2015 Jun 23; 54(24):3749-58. PMID: 26042961; PMCID: PMC4743497; DOI: 10.1021/acs.biochem.5b00330;.
  10. Bewley KD, Dey M, Bjork RE, Mitra S, Chobot SE, Drennan CL, Elliott SJ. Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials. PLoS One. 2015; 10(4):e0122466.View Related Profiles. PMID: 25874934; PMCID: PMC4395160; DOI: 10.1371/journal.pone.0122466;.
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This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 52 publications over 16 distinct years, with a maximum of 8 publications in 2012

In addition to these self-described keywords below, a list of MeSH based concepts is available here.

Bioinorganic Chemistry
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