Sean Elliott, PhD
Boston University College of Arts and Sciences

PhD, California Institute of Technology
BA, Amherst College

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.

Boston University
Evans Center for Interdisciplinary Biomedical Research

Graduate Studies Director
Boston University College of Arts and Sciences

Redox Cofactor Diversity in Enzymatic Superfamilies
06/01/2020 - 05/31/2025 (PI)
NIH/National Institute of General Medical Sciences

Tuning Directionality for CO2 Reduction in the Oxo-Acid: Ferredoxin Superfamily
09/01/2014 - 08/31/2024 (PI)
Department of Energy

Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family
01/01/2017 - 12/31/2021 (PI)
NIH/National Institute of General Medical Sciences

Redox Reactions of the AdoMet Radical Enzyme Superfamily
08/15/2016 - 06/30/2021 (PI)
NIH/National Institute of General Medical Sciences

Structure-function relationships in metalloenzymes with multiple redox-active centers
09/01/2016 - 05/31/2020 (Subcontract PI)
University of Wisconsin System National Science Fdn

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 (Subcontract 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

Showing 10 of 11 results. Show All Results


Yr Title Project-Sub Proj Pubs
2023 Redox Cofactor Diversity in Enzymatic Superfamilies 5R35GM136294-04
2023 Redox Cofactor Diversity in Enzymatic Superfamilies 3R35GM136294-04S1
2022 Redox Cofactor Diversity in Enzymatic Superfamilies 5R35GM136294-03
2021 Redox Cofactor Diversity in Enzymatic Superfamilies 5R35GM136294-02
2020 Redox Cofactor Diversity in Enzymatic Superfamilies 1R35GM136294-01
2020 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 5R01GM110390-04 2
2019 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 5R01GM110390-03 2
2019 Redox Reactions of the AdoMet Radical Enzyme Superfamily 5R01GM120283-04 5
2018 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 5R01GM110390-02 2
2018 Redox Reactions of the AdoMet Radical Enzyme Superfamily 5R01GM120283-03 5
Showing 10 of 19 results. Show All Results

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.

iCite Analysis       Copy PMIDs To Clipboard

  1. Paris JC, Hu S, Wen A, Weitz AC, Cheng R, Gee LB, Tang Y, Kim H, Vegas A, Chang WC, Elliott SJ, Liu P, Guo Y. An S=1 Iron(IV) Intermediate Revealed in a Non-Heme Iron Enzyme-Catalyzed Oxidative C-S Bond Formation. Angew Chem Int Ed Engl. 2023 Oct 23; 62(43):e202309362.View Related Profiles. PMID: 37640689; PMCID: PMC10592081; DOI: 10.1002/anie.202309362;
  2. Gupta D, Chen K, Elliott SJ, Nayak DD. MmcA is an electron conduit that facilitates both intracellular and extracellular electron transport in Methanosarcina acetivorans. bioRxiv. 2023 Apr 20. PMID: 37131651; PMCID: PMC10153276; DOI: 10.1101/2023.04.20.537704;
  3. Hu WY, Li K, Weitz A, Wen A, Kim H, Murray JC, Cheng R, Chen B, Naowarojna N, Grinstaff MW, Elliott SJ, Chen JS, Liu P. Light-driven Oxidative Demethylation Reaction Catalyzed by a Rieske-type Non-heme Iron Enzyme Stc2. ACS Catal. 2022 Dec 02; 12(23):14559-14570.View Related Profiles. PMID: 37168530; PMCID: PMC10168674; DOI: 10.1021/acscatal.2c04232;
  4. Cheng R, Weitz AC, Paris J, Tang Y, Zhang J, Song H, Naowarojna N, Li K, Qiao L, Lopez J, Grinstaff MW, Zhang L, Guo Y, Elliott S, Liu P. OvoAMtht from Methyloversatilis thermotolerans ovothiol biosynthesis is a bifunction enzyme: thiol oxygenase and sulfoxide synthase activities. Chem Sci. 2022 Mar 24; 13(12):3589-3598.View Related Profiles. PMID: 35432880; PMCID: PMC8943887; DOI: 10.1039/d1sc05479a;
  5. Pang H, Walker LM, Silakov A, Zhang P, Yang W, Elliott SJ, Yokoyama K. Mechanism of Reduction of an Aminyl Radical Intermediate in the Radical SAM GTP 3',8-Cyclase MoaA. J Am Chem Soc. 2021 09 01; 143(34):13835-13844. PMID: 34423974; PMCID: PMC8415136; DOI: 10.1021/jacs.1c06268;
  6. Sosa Alfaro V, Campeciño J, Tracy M, Elliott SJ, Hegg EL, Lehnert N. Elucidating Electron Storage and Distribution within the Pentaheme Scaffold of Cytochrome c Nitrite Reductase (NrfA). Biochemistry. 2021 06 15; 60(23):1853-1867. PMID: 34061493
  7. Zhu W, Walker LM, Tao L, Iavarone AT, Wei X, Britt RD, Elliott SJ, Klinman JP. Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters in Methylorubrum extorquens PqqE. J Am Chem Soc. 2020 07 22; 142(29):12620-12634. PMID: 32643933; PMCID: PMC7398046; DOI: 10.1021/jacs.0c02044;
  8. Rizzolo K, Weitz AC, Cohen SE, Drennan CL, Hendrich MP, Elliott SJ. A Stable Ferryl Porphyrin at the Active Site of Y463M BthA. J Am Chem Soc. 2020 07 15; 142(28):11978-11982. PMID: 32564595; PMCID: PMC8667324; DOI: 10.1021/jacs.0c04023;
  9. Weitz AC, Biswas S, Rizzolo K, Elliott S, Bominaar EL, Hendrich MP. Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis. Inorg Chem. 2020 Jul 20; 59(14):10223-10233. PMID: 32602712; PMCID: PMC8049104; DOI: 10.1021/acs.inorgchem.0c01349;
  10. Hamby H, Li B, Shinopoulos KE, Keller HR, Elliott SJ, Dukovic G. Light-driven carbon-carbon bond formation via CO2 reduction catalyzed by complexes of CdS nanorods and a 2-oxoacid oxidoreductase. Proc Natl Acad Sci U S A. 2020 01 07; 117(1):135-140. PMID: 31852819; PMCID: PMC6955356; DOI: 10.1073/pnas.1903948116;
Showing 10 of 71 results. Show More

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 71 publications over 21 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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