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.

Member
Boston University
Evans Center for Interdisciplinary Biomedical Research


Graduate Studies Director
Boston University College of Arts and Sciences
Chemistry




Redox Cofactor Diversity in Enzymatic Superfamilies
06/01/2020 - 05/31/2025 (PI)
NIH/National Institute of General Medical Sciences
1R35GM136294-01

Tuning Directionality for CO2 Reduction in the Oxo-Acid: Ferredoxin Superfamily
09/01/2014 - 08/31/2021 (PI)
Department of Energy
DE-SC00112598

Redox Reactions of the AdoMet Radical Enzyme Superfamily
08/15/2016 - 06/30/2021 (PI)
NIH/National Institute of General Medical Sciences
5R01GM120283-04

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
5R01GM110390-04

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
MCB-1616824

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 (Subcontract PI)
Pennsylvania State University NIH NIGMS
5R01GM103268-04

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


Showing 10 of 11 results. Show All Results


Title


Yr Title Project-Sub Proj Pubs
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
2017 Structure, Function and Diversity in the Bacterial Cytochrome c Peroxidase Family 1R01GM110390-01A1 2
2017 Redox Reactions of the AdoMet Radical Enzyme Superfamily 5R01GM120283-02 5
2016 Redox Reactions of the AdoMet Radical Enzyme Superfamily 1R01GM120283-01 5
2010 The Electrochemistry of Diheme Cytochrome c Peroxidases 5R01GM072663-05 15
Showing 10 of 15 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. 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 Jul 22; 142(29):12620-12634. PMID: 32643933
     
  2. 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 Jul 15; 142(28):11978-11982. PMID: 32564595
     
  3. 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
     
  4. 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
     
  5. Walker LM, Li B, Niks D, Hille R, Elliott SJ. Deconvolution of reduction potentials of formate dehydrogenase from Cupriavidus necator. J Biol Inorg Chem. 2019 09; 24(6):889-898. PMID: 31463592
     
  6. Rizzolo K, Cohen SE, Weitz AC, López Muñoz MM, Hendrich MP, Drennan CL, Elliott SJ. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Nat Commun. 2019 03 07; 10(1):1101. PMID: 30846684
     
  7. 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 02 19; 58(7):940-950. PMID: 30628436
     
  8. Chen PY, Li B, Drennan CL, Elliott SJ. A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO2. Joule. 2019 Feb 20; 3(2):595-611. PMID: 31080943
     
  9. 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 01; 28(1):267-282. PMID: 30394621
     
  10. Maiocco SJ, Arcinas AJ, Booker SJ, Elliott SJ. Parsing redox potentials of five ferredoxins found within Thermotoga maritima. Protein Sci. 2019 01; 28(1):257-266. PMID: 30418685
     
Showing 10 of 65 results. Show More

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

Bar chart showing 65 publications over 18 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
20197
20203

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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