Sean Elliott, PhD
Professor
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
5R01GM110390-02

REDOX REACTIONS OF THE ADOMET RADICAL ENZYME SUPERFAMILY
08/15/2016 - 06/30/2020 (PI)
NIH/National Institute of General Medical Sciences
5R01GM120283-03

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
DE-SC00112598

CONNECTIONS BETWEEN REDOX CHEMISTRY AND CATALYSIS IN MULTIHEME PEROXIDASES
09/01/2013 - 08/31/2017 (PI)
National Science Foundation
CHE-1310012

FUNCTIONALIZATION OF UNACTIVATED SP2-HYBRIDIZED CARBON ATOMS
07/01/2014 - 06/30/2017 (PI)
Pennsylvania State University NIH NIGMS
5R01GM103268

REDOX REACTIVITY OF THIROREDOXIN DISULFIDE BONDS
08/01/2011 - 07/31/2016 (PI)
National Science Foundation
MCB-1122977

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
5F31GM099416-04

PHOTO-INDUCED CO2 REDUCTION USING REVERSE TCA CYCLE ENZYMES
01/01/2013 - 12/31/2014 (PI)
Research Corporation for Science Advancement

HYBRID METAMATERIALS FOR SOLAR BIOFUEL GENERATION
07/01/2010 - 06/30/2013 (PI)
City College of New York DOD AFOSR




Yr Title Project-Sub Proj Pubs
2019 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 5R01GM110390-03
2018 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 5R01GM110390-02
2018 Redox Reactions of the AdoMet Radical Enzyme Superfamily 5R01GM120283-03
2017 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 1R01GM110390-01A1
2016 Redox Reactions of the AdoMet Radical Enzyme Superfamily 1R01GM120283-01
2010 The Electrochemistry of Diheme Cytochrome c Peroxidases 5R01GM072663-05 13
2009 The Electrochemistry of Diheme Cytochrome c Peroxidases 3R01GM072663-04S1 13
2009 The Electrochemistry of Diheme Cytochrome c Peroxidases 5R01GM072663-04 13
2008 The Electrochemistry of Diheme Cytochrome c Peroxidases 5R01GM072663-03 13
2007 The Electrochemistry of Diheme Cytochrome c Peroxidases 5R01GM072663-02 13
Showing 10 of 11 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.

  1. Ayikpoe R, Ngendahimana T, Langton M, Bonitatibus S, Walker LM, Eaton SS, Eaton GR, Pandelia ME, Elliott SJ, Latham JA. Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insight into its redox flipping mechanism. Biochemistry. 2019 Jan 10. PMID: 30628436.
     
  2. Maiocco SJ, Arcinas AJ, Booker SJ, Elliott SJ. Parsing redox potentials of five ferredoxins found within Thermotoga maritima. Protein Sci. 2019 Jan; 28(1):257-266. PMID: 30418685.
     
  3. Arcinas AJ, Maiocco SJ, Elliott SJ, Silakov A, Booker SJ. Ferredoxins as interchangeable redox components in support of MiaB, a radical S-adenosylmethionine methylthiotransferase. Protein Sci. 2019 Jan; 28(1):267-282. PMID: 30394621.
     
  4. Atkinson JT, Campbell IJ, Thomas EE, Bonitatibus SC, Elliott SJ, Bennett GN, Silberg JJ. Metalloprotein switches that display chemical-dependent electron transfer in cells. Nat Chem Biol. 2018 Dec 17. PMID: 30559426.
     
  5. Wolf MW, Rizzolo K, Elliott SJ, Lehnert N. Resonance Raman, Electron Paramagnetic Resonance, and Magnetic Circular Dichroism Spectroscopic Investigation of Diheme Cytochrome c Peroxidases from Nitrosomonas europaea and Shewanella oneidensis. Biochemistry. 2018 Nov 13; 57(45):6416-6433. PMID: 30335984.
     
  6. Walker LM, Kincannon WM, Bandarian V, Elliott SJ. Deconvoluting the Reduction Potentials for the Three [4Fe-4S] Clusters in an AdoMet Radical SCIFF Maturase. Biochemistry. 2018 Oct 23; 57(42):6050-6053. PMID: 30272955.
     
  7. 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 Oct; 23(7):1073-1083. PMID: 30143872.
     
  8. 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.
     
  9. 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.
     
  10. 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.
     
Showing 10 of 58 results. Show More

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

Bar chart showing 58 publications over 17 distinct years, with a maximum of 8 publications in 2012

YearPublications
20022
20031
20042
20052
20062
20074
20084
20093
20101
20115
20128
20133
20145
20155
20163
20185
20193
In addition to these self-described keywords below, a list of MeSH based concepts is available here.

Bioinorganic Chemistry
Electrochemistry
Bioenergy
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Boston MA 02215
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