63. Zhu W, Walker LM, Tao L, Iavarone AT, Wei X, Britt RD, Elliott SJ, Klinman J, “Structural Properties and Catalytic Implications of the SPASM Domain Iron–Sulfur Clusters in Methylorubrum extorquens PqqE”, J. Am. Chem. Soc., 2020, 142(29), 12620- 12634. [DOI]

62. Weitz AC, Biswas S, Rizzolo K, Elliott SJ, Bominaar EL, Hendrich MP. “Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis”, Inorg. Chem., 2020, 59(14), 10223-10233. [DOI]

61. 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, 142(28), 11978-11982. [DOI]

60. Hamby H, Li B, Shinopoulos KE, Keller HR, Elliott SJ, Dukovic G. “Light-driven carbon-carbon bond formation of CO2 reduction catalyzed by complexes of nanorods and a 2-oxoacid oxidoreductase”, Proc. Natl. Acad. Sci., 2020, 117(1): 135-140. [DOI]


59. Walker LM, Li B, Niks D, Hille R, Elliott SJ. “Deconvoluting the redox potentials of formate dehydrogenase”, J. Biol. Inorganic Chemistry. 2019,24(6):889-898. [DOI]

58. Rizzolo KR, Weitz AC, Cohen SE, López Muñoz ML, Hendrich MP, Drennan CL, Elliott SJ. “A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis- Fe(IV) state”, Nature Communications, 2019, 1101. [DOI]

57. Ayikpoe R, Ngendahimana T, Langton M, Bonitatibus S, Walker LM, Eaton S, Eaton G, Pandelia M-E, Elliott SJ, Latham J, “ Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insightt into its redox flipping mechanism”, Biochemistry, 2019, 58(7) 940-950. [DOI]

56. Chen PYT, Li B, Drennan CL, Elliott SJ, “A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO₂”, Joule, 2019, 3(2), 595-611. [DOI]

55. Maiocco SJ, Arcinas AJ, Booker SJ, Elliott SJ, “Parsing redox potentials of five ferredoxins found within Thermotoga maritima”, Protein Science, 2019, 26: 257-266. [DOI]

54. 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 Science, 2019, 26: 267–282. [DOI]

53. Atkinson JT, Campbell IJ, Thomas EE, Bonitatibus SC, Elliott SJ, Bennett GN, Silberg JJ. “Metalloprotein switches that display chemical-dependent electron transfer in cells”, Nature – Chemical Biology, 2019, 15, 189-195 [DOI]


52. Wolf M, Rizzolo K, Elliott SJ, Lehnert N, “Resonance Raman, EPR and MCD Spectroscopic Investigation of Diheme Cytochrome c Peroxidases from Nitrosomonas europaea and Shewanella oneidensis,” Biochemistry, 2018, 57 (45): 6416–6433.

51. 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, 57(42):6050-6053.

50. Kleingarden JG, Levin BD, Zoppellaro G, Andersson KK, Elliott SJ, Bren KL, “Influence of heme c attachment on heme conformation and potential,” Journal of Biological Inorganic Chemistry, 2018, 1-11

49. Maiocco SJ, Walker LM, Elliott SJ, “Determining redox potential of the Iron-sulfur clusters of the AdoMet Radical Enzyme Superfamily,” in Methods in Enzymology, V Bandarian, et., 2018, 606, 319-339


48. Ceccaldi P, Schuchmann K, Müller V, Elliott SJ, “The hydrogen dependent CO2 reductase: the first completely CO tolerant FeFe-hydrogenase,” Energy and Environmental Science , 2017, 10, 503-508. [DOI]


47. Maiocco SJ, Arcinas A, Landgraf B, Lee K-H, Booker SJ, Elliott SJ, “Transformations of the FeS clusters of the methylthiotransferases MiaB and RimO, detected by direct electrochemistry,” Biochemistry, 2016, 55(39), 5531-5536. [DOI]

46. Dowling D, Miles Z, Köhrer C, Maiocco SJ, Elliott SJ, Bandarian V, Drennan, CL. “Molecular basis of Cobalamin-dependent RNA modification”, Nucleic Acids Research, 2016, 44(20):9965-9976. [DOI]

45. 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, 138(10), 3416-3426. [DOI]

44. Li B and Elliott SJ. “The catalytic bias of 2-oxoacid:ferredoxin oxidoreductase in CO2 evolution and reduction through a ferredoxin-mediated electrochemical assay,” Electrochimica Acta, 2016, 199, 349-356. [DOI]


43.  Frato KE, Walsh KW, Elliott SJ. “Functionally distinct bacterial cytochrome c peroxidases proceed through a common (electro)catalytic intermediate,” Biochemistry, 2015, 55(1),125-132. [DOI]

42. Wei Y, Li B, Prakash D, Ferry J, Elliott SJ, Stubbe J. “A ferredoxin disulfide reductase delivers electrons to the Methanosarcina barkeri class III ribonucleotide reductase,” Biochemistry, 2015, 54(47), 7019-7028. [DOI]

41. Stein N, Love D, Judd ET, Elliott SJ, Bennett B, Pacheco AA. “Correlations between the Electronic Properties of Shewanella oneidensis Cytochrome c Nitrite Reductase and Its Structure: Effects of Heme Oxidation State and Active Site Ligation,” Biochemistry, 2015, 54(24): 3749-58. [DOI]

40. 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, 127(37): 8664-8667. [DOI]

39. Bewley KD, Dey M, Mitra S, Chobot SE, Drennan CL and Elliott SJ. “Rheostat re-wired: tuning reduction potentials of disulfide bonds independently of Cys pKas”, PLOS-One, 2015. [DOI]

38. Levin BD, Walsh KA, Sullivan KK, Bren KL, Elliott SJ, “Methionine Ligand Lability of Homologous Monoheme Cytochromes c”, Inorganic Chemistry, 2015, 54 (1):38-46. [DOI]


37. Hu W, Song H, Sae Her A, Bak DW, Naowarojna N, Elliott SJ, Qin L, Chen X, Liu P,
“Bioinformatic and Biochemical Characterizations of C-S Bond Formation and Cleavage Enzymes in the Fungus Neurospora crassa Ergothioneine Biosynthetic  Pathway,” Organic Letter, 2014, 16(20): 5382-5385. [DOI]

36. Judd ET,  Stein N, Pacheco AA, Elliott SJ, “Hydrogen Bonding Networks Tune Proton-Coupled
Redox Steps During the Enzymatic Six-electron Conversion of Nitrite to Ammonia,” Biochemistry, 2014, 53 (35): 5638-5646. [DOI]

35. Funk MA, Judd ET, Marsh ENG, Elliott SJ, Drennan CL, “Structures of benzylsuccinate synthase
elucidate roles of accessory subunits in glycyl radical enzyme activation and activity,” Proc. Natl. Acad. Sci. , 2014, 111(28): 10161-10166. [DOI]

34. Bak DW and Elliott SJ, “Alternative FeS cluster ligands: tuning redox potentials and chemistry,” Current Opinions in Chemical Biology, 2014, 19: 50-58. [DOI]


33. Bak DW and Elliott SJ, “Conserved hydrogen bond networks tune FeS cluster binding and structural stability,” Biochemistry, 2013, 52(27): 4687-4696. [PDF]

32. Duncan GGM, Marritt SJ, Firer-Sherwood MA, Shi L, Richardson DJ, Evans SD, Elliott SJ,
Butt JN, Jeuken LJC. “Protein-Protein Interaction Regulates the Direction of Catalysis and Electron Transfer in a Redox Enzyme Complex,” J. Am. Chem. Soc., 2013,135 (28):10550-10556. [DOI]

31. Bewley KD, Ellis KE, Firer-Sherwood MA, Elliott SJ. “Multi-heme proteins: Nature’s electronic multi-purpose tool,” Biochimica et Biophysica Acta – Bioenergetics, 2013, 1827 (8-9): 938-94. [DOI]


30. Judd ET, Youngblut M, Pacecho AA, Elliott SJ. “Direct electrochemistry of Shewanella oneidensis cytochrome c nitrite reductase: evidence for interactions across the dimeric interface,” Biochemistry, 2012, 51 (51):10175-85. [PDF]

29. Ellis KE, Frato KE, Elliott SJ. “Impact of Quarternary Structure upon Bacterial Cytochrome c Peroxidases: does homodimerization matter?” Biochemistry, 2012, 51(50): 10008-10016. [PDF]

28. Hamill MJ, Jost M, Wong C, Bene NC*, Drennan CL, Elliott SJ. “Electrochemical characterization of Escherichia coli adaptive response protein AidB”, International Journal of Molecular Sciences, 2012, 13(12), 16899-16915. [DOI]

27. Bewley KD, Firer-Sherwood MA, Mock JY*, Ando N, Drennan CL, Elliott SJ. “Mind the gap: diversity and reactivity of multiheme cytochromes of the MtrA/DmsE family,” Transactions of the Biochemical Society, 2012, 40(6), 1268-1273. [DOI]

26. Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, Elliott SJ, Drennan CL. “Unusual Role for a Mobile Flavin in a StaC-like Indolocarbazole Biosynthetic Enzyme,” Chemistry & Biology, 2012, 19(7), 855-865. [DOI]

25. Seidel J, Hoffmann M, Ellis KE, Seidel A, Spatzal T, Gerhardt S, Elliott SJ, Einsle O. “MacA is a Second Cytochrome c Peroxidase of Geobacter sulfurreducens”, Biochemistry, 2012, 50(21), 4513-20. [PDF]

24. Youngblut M, Judd EJ, Srajer V, Sayyed B, Groelzer T, Elliott SJ, Schmidt M, Pacheco AA. “Laue crystal structure of Shewanella oneidensis cytochrome c nitrite reductase from a high-yield expression system”, Journal of Biological Inorganic Chemistry, 2012, 17(4), 674-662. [PDF]

23. Pulcu GS,  Frato KE, Gupta R, Hsu H.-R., Levine GA, Hendrich MP, Elliott SJ. “The Cytochrome c Peroxidase from Shewanella oneidensis Requires Reductive Activation,” Biochemistry, 2012, 52: 974-985. [ PDF ]


22. Hamill, M.J.; Jost, M.; Wong, C.Y.; Elliott, S.J.; Drennan, C.L. “Flavin Induced Oligomerization in Escherichia coli Adaptive Response Protein AidB,” Biochemistry, 2011, 51: 10159-10169. [ PDF ]

21. Levin, B.D.; Can, M.; Bren, K.L.; Elliott, S.J. “Methionine Lability in Bacterial Monoheme Cytochromes c: an electrochemical study,” Journal of Physical Chemistry – B, 2011, 11718-11726. [ PDF ]

20. Firer-Sherwood, M.A.; Ando, N.; Drennan, C.L.; Elliott, S.J. “Solution-based Structural
Analysis of the Decaheme Cytochrome MtrA, by Small Angle X-Ray Scattering and Analytical Ultracentrifugation,” J. Phys. Chem.  – B, 2011, 11208-1114. [PDF]

19. Ellis, K.E.; Seidel, J.; Einsle, O.; Elliott, S.J. “Geobacter sulfurreducens Cytochrome c Peroxidases: electrochemical classification of catalytic mechanisms,” Biochemistry, 2011, 51: 4513-4520. [PDF]

18. Firer-Sherwood, M.A.; Bewley, K.D.; Mock, J.Y.; Elliott, S.J. “Tools for Resolving Complexity in the Electron Transfer Networks of Multiheme Cytochromes” Metallomics, 2011, 3:344-348. [PDF]


17. Cong, H.; Becker, C.F.; Elliott, S.J.; Grinstaff, M.W.; Porco, J.A. “Silver Nanoparticle-Catalyzed Diels-Alder Cycloadditions of 2’-Hydroxychalcones”. J. Am. Chem. Soc. 2010, 132:7514-7518. [PDF]


16. Bak, D.W.; Zuris, J.A.; Paddock, M.; Jennings, P.A.; Elliott, S.J.  “Redox Characterization of the FeS Protein MitoNEET and impact of thiazolidinedione drug binding.” Biochemistry 2009, 48(43):10193-5. [PDF]

15.  Mitra, S.; Elliott, S.J. “Oxidative Disassembly of the [2Fe-2S] Cluster of Human Glutaredoxin 2 and Redox Regulation in the Mitochrondria.” Biochemistry 2009, 48(18):3813-3815. [PDF]

14. Becker, C.F.; Watmough, N.J.; Elliott, S.J. “Electrochemical Evidence for Multiple Peroxidatic Heme States of the Diheme Cytochrome c Peroxidase of Pseudomonas aeruginosa.Biochemistry 2009, 48(1):87-95.[PDF]


13. Hamill, M.J.; Chobot, S.E.; Hernandez, H.H.; Drennan, C.L.; Elliott, S.J. m”Direct Electrochemical Analyses of a Thermophilic Thioredoxin Reductase: interplay between conformational change and redox chemistry.” Biochemistry 2008, 47(37):9738-9746. [PDF]

12. Hernandez, H.H.; Jaquez, O.; Hamill, M.J.; Elliott, S.J.; Drennan, C.L.  “Thioredoxin reductase from Thermoplasma acidophilum: a new twist on redox regulation” Biochemistry 2008, 47(37):9728-9737. [PDF]

11. Firer-Sherwood, M.; Pulcu, G.S.; Elliott, S.J. “Electrochemical interrogations of the Mtr cytochromes from Shewanella: opening a potential window.” J. Biol. Inorg. Chem. 2008, 13(6):849-854. [PDF]

10. Ye, T.; Kaur, R.; Senguen, F.T.; Michel, L.V.; Bren, K.L.; Elliott, S.J.  “Methionine ligand lability of type I cytochromes c: detection of ligand loss using protein film voltammetry.” J. Am. Chem. Soc. 2008 130(21):6682-3. [PDF]


9. Michel, L.V.; Ye, T.; Bowman, S.E.; Levin, B.D.; Hahn, M.A.; Russell, B.S.; Elliott, S.J.; Bren, K.L.
“Heme attachment motif mobility tunes cytochrome c redox potential.” Biochemistry 2007 46(42), 11753-60. [PDF]

8.  Ryan, K.S.; Howard-Jones, A.R.; Hamill, M.J.; Elliott, S.J.; Walsh, C.T.; Drennan, C.L.
“Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC.” Proc. Natl. Acad. Sci. USA 2007 104(39), 15311-6. [PDF]

7. Chobot, S.E.; Hernandez, H.H.; Drennan, C.L.; Elliott, S.J.  “Direct Electrochemical Characterization of Archaeal Thioredoxins.” Angew. Chemie 2007, 46(22), 4145-7.

6. Pulcu, G.S.; Elmore, B.L.; Arciero, D.M.; Hooper, A.B.; Elliott, S.J. “Direct electrochemistry of tetraheme cytochrome c-554 from Nitrosomonas europaea: Redox cooperativity and conformational gating” J. Am. Chem. Soc. 2007, 129(7),1838-9. [PDF]

5. Bradley, A.L; Arciero, D.M.; Hooper, A.B.; Elliott, S.J.
“Protonation and inhibition of Cytochrome c Peroxidase from Nitrosomonas europaea“. J. Inorg. Biochem. 2007, 101(1), 1733-39. [PDF]


4. Tarasev, M.; Pinto, A.; Kim, D.; Elliott, S.J.; Ballou, D.P.  “The ‘bridging’ aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron (II)-mononuclear
center”. Biochemistry 2006, 45(34): 10208-16. [PDF]


3. Ye, T.; Kaur, R.; Wen, X.; Bren, K.L. Elliott, S.J. “Redox properties of wild-type and heme-binding loop mutants of bacterial cytochromes c measured by direct electrochemistry”. Inorg. Chem. 2005, 44(24): 8999-9006. [PDF]

2. di Bernardo, D.; Thompson, M.J.; Gardner, T.S.; Chobot, S.E.*; Eastwood, E.L.; Wojtovich,
A.P.; Elliott, S.J.; Schaus, S.E.; Collins, J.J.  “Chemogenomic Profiling on a Genome-wide Scale Using Reverse-Engineered Gene Networks”. Nature-Biotechnology, 2005, 23(3), 377-83.


1. Bradley, A.L.; Chobot, S.E.; Arciero, D.M.; Hooper, A.B.; Elliott, S.J..
“A Distinctive Electrocatalytic Response from the Cytochrome c Peroxidase of Nitrosomonas europaea“. J. Biol. Chem. 2004, 279(14): 13297-13300. [ PDF]