{"id":47,"date":"2017-06-27T16:36:40","date_gmt":"2017-06-27T20:36:40","guid":{"rendered":"https:\/\/sites.bu.edu\/sje-lab\/?page_id=47"},"modified":"2021-01-05T13:29:11","modified_gmt":"2021-01-05T18:29:11","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.bu.edu\/sje-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

2020<\/h3>\n

63. Zhu W, Walker LM, Tao L, Iavarone AT, Wei X, Britt RD, Elliott SJ, Klinman J, \u201cStructural Properties and Catalytic Implications of the SPASM Domain Iron\u2013Sulfur Clusters in Methylorubrum extorquens PqqE”, J. Am. Chem. Soc., 2020, 142(29), 12620- 12634. [DOI]<\/a><\/p>\n

62. Weitz AC, Biswas S, Rizzolo K, Elliott SJ, Bominaar EL, Hendrich MP. \u201cElectronic State of the His\/Tyr-Ligated Heme of BthA by M\u00f6ssbauer and DFT Analysis\u201d, Inorg. Chem., 2020, 59(14), 10223-10233. [DOI]<\/a><\/p>\n

61. Rizzolo K, Weitz AC, Cohen SE, Drennan CL, Hendrich MP, Elliott SJ. \u201cA Stable Ferryl Porphyrin at the Active Site of Y463M BthA\u201d, J. Am. Chem. Soc., 2020, 142(28), 11978-11982. [DOI]<\/a><\/p>\n

60. Hamby H, Li B, Shinopoulos KE, Keller HR, Elliott SJ, Dukovic G. \u201cLight-driven carbon-carbon bond formation of CO2 reduction catalyzed by complexes of nanorods and a 2-oxoacid oxidoreductase\u201d, Proc. Natl. Acad. Sci., 2020, 117(1): 135-140. [DOI]<\/a><\/p>\n

2019<\/h3>\n

59. Walker LM, Li B, Niks D, Hille R, Elliott SJ. \u201cDeconvoluting the redox potentials of formate dehydrogenase\u201d, J. Biol. Inorganic Chemistry. 2019,24(6):889-898. [DOI]<\/a><\/p>\n

58. Rizzolo KR, Weitz AC, Cohen SE, L\u00f3pez Mu\u00f1oz ML, Hendrich MP, Drennan CL, Elliott SJ. \u201cA widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis- Fe(IV) state\u201d, Nature Communications, 2019, 1101. [DOI]<\/a><\/p>\n

57. Ayikpoe R, Ngendahimana T, Langton M, Bonitatibus S, Walker LM, Eaton S, Eaton G, Pandelia M-E, Elliott SJ, Latham J, \u201c Spectroscopic and electrochemical characterization of the mycofactocin biosynthetic protein, MftC, provides insightt into its redox flipping mechanism\u201d, Biochemistry, 2019, 58(7) 940-950. [DOI]<\/a><\/p>\n

56. Chen PYT, Li B, Drennan CL, Elliott SJ, \u201cA reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO\u2082\u201d, Joule, 2019, 3(2), 595-611. [DOI]<\/a><\/p>\n

55. Maiocco SJ, Arcinas AJ, Booker SJ, Elliott SJ, \u201cParsing redox potentials of five ferredoxins found within Thermotoga maritima\u201d, Protein Science, 2019, 26: 257-266. [DOI]<\/a><\/p>\n

54. Arcinas AJ, Maiocco SJ, Elliott SJ, Silakov A, Booker SJ,\u201cFerredoxins as interchangeable redox components in support of MiaB, a radical S-adenosylmethionine methylthiotransferase\u201d, Protein Science, 2019, 26: 267\u2013282. [DOI]<\/a><\/p>\n

53. Atkinson JT, Campbell IJ, Thomas EE, Bonitatibus SC, Elliott SJ, Bennett GN, Silberg JJ. \u201cMetalloprotein switches that display chemical-dependent electron transfer in cells\u201d, Nature – Chemical Biology, 2019, 15, 189-195 [DOI]<\/a><\/p>\n

2018<\/h3>\n

52. Wolf M, Rizzolo K, Elliott SJ, Lehnert N, \u201cResonance Raman, EPR and MCD Spectroscopic Investigation of Diheme Cytochrome c Peroxidases from Nitrosomonas europaea and Shewanella oneidensis,\u201d Biochemistry, 2018, 57 (45): 6416\u20136433.<\/p>\n

51. Walker LM, Kincannon WM, Bandarian V, Elliott SJ, \u201cDeconvoluting the reduction potentials for the three [4Fe\u20144S] clusters in an AdoMet Radical SCIFF maturase,\u201d Biochemistry, 2018, 57(42):6050-6053.<\/p>\n

50. Kleingarden JG, Levin BD, Zoppellaro G, Andersson KK, Elliott SJ, Bren KL, \u201cInfluence of heme c attachment on heme conformation and potential,\u201d Journal of Biological Inorganic Chemistry, 2018, 1-11<\/p>\n

49. Maiocco SJ, Walker LM, Elliott SJ, \u201cDetermining redox potential of the Iron-sulfur clusters of the AdoMet Radical Enzyme Superfamily,\u201d in Methods in Enzymology, V Bandarian, et., 2018, 606, 319-339<\/p>\n

2017<\/h3>\n

48. Ceccaldi P, Schuchmann K, M\u00fcller V, Elliott SJ, \u201cThe hydrogen dependent CO2 reductase: the first completely CO tolerant FeFe-hydrogenase,\u201d Energy and Environmental Science , 2017, 10, 503-508. [DOI<\/a>]<\/p>\n

2016<\/h3>\n

47. Maiocco SJ, Arcinas A, Landgraf B, Lee K-H, Booker SJ, Elliott SJ, \u201cTransformations of the FeS clusters of the methylthiotransferases MiaB and RimO, detected by direct electrochemistry,\u201d Biochemistry<\/em>, 2016<\/strong>, 55<\/em>(39), 5531-5536. [DOI<\/a>]<\/p>\n

46. Dowling D, Miles Z, K\u00f6hrer C, Maiocco SJ, Elliott SJ, Bandarian V, Drennan, CL. \u201cMolecular basis of Cobalamin-dependent RNA modification\u201d, Nucleic Acids Research,<\/em> 2016<\/strong>, 44<\/em>(20):9965-9976. [DOI<\/a>]<\/p>\n

45. Blaszczyk AJ, Silakov A, Zhang B, Maiocco SJ, Lanz ND, Kelly WL, Elliott SJ, Krebs C, Booker SJ. \u201cSpectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase\u201d, J. Am. Chem. Soc.<\/em> 2016<\/strong>, 138<\/em>(10), 3416-3426. [DOI<\/a>]<\/p>\n

44. Li B and Elliott SJ. \u201cThe catalytic bias of 2-oxoacid:ferredoxin oxidoreductase in CO2 evolution and reduction through a ferredoxin-mediated electrochemical assay,\u201d Electrochimica Acta<\/em>, 2016<\/strong>, 199, 349-356. [DOI<\/a>]<\/p>\n

2015<\/h3>\n

43.\u00a0 Frato KE, Walsh KW, <\/span>Elliott SJ<\/span>. \u201cFunctionally distinct bacterial cytochrome c peroxidases proceed through a common (electro)catalytic intermediate,\u201d Biochemistry<\/em>, <\/span>2015<\/span><\/strong>, 55<\/em>(1),125-132. [<\/span>DOI<\/a>]<\/span>
\n<\/span><\/p>\n

42. Wei Y, Li B, Prakash D, Ferry J, <\/span>Elliott SJ<\/span>, Stubbe J. \u201cA ferredoxin disulfide reductase delivers electrons to the Methanosarcina barkeri<\/em> class III ribonucleotide reductase,\u201d Biochemistry<\/em>, <\/span>2015<\/span><\/strong>, 54<\/em>(47), 7019-7028. [<\/span>DOI<\/a>]<\/span><\/p>\n

41. Stein N, Love D, Judd ET, Elliott SJ<\/span>, Bennett B, Pacheco AA. \u201cCorrelations between the Electronic Properties of Shewanella oneidensis <\/span>Cytochrome c<\/span> Nitrite Reductase and Its Structure: Effects of Heme Oxidation State and Active Site Ligation,\u201d Biochemistry<\/span><\/em>, 2015<\/span><\/strong>, 54<\/em>(24): 3749-58. <\/span>[DOI<\/a>]<\/p>\n

40. Maiocco SJ, Grove TL, Booker SJ, <\/span>Elliott SJ<\/span>. \u201cElectrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low- Potential Auxiliary Cluster,\u201d J. Am. Chem. Soc<\/em>. , <\/span>2015<\/span><\/strong>, 127<\/em>(<\/span>37<\/span>): 8664-8667. [<\/span>DOI<\/a>]
\n<\/span><\/p>\n

39. Bewley KD, Dey M, Mitra S, Chobot SE, Drennan CL and <\/span>Elliott SJ<\/span>. \u201cRheostat re-wired: tuning reduction potentials of disulfide bonds independently of Cys pK<\/span>a<\/span>s\u201d, PLOS-One<\/em>, <\/span>2015<\/span><\/strong>. [<\/span>DOI<\/a>]<\/span> <\/span><\/p>\n

38. Levin BD, Walsh KA, Sullivan KK, Bren KL, Elliott SJ, \u201cMethionine Ligand Lability of Homologous Monoheme Cytochromes c<\/span>\u201d, Inorganic Chemistry<\/em>, <\/span>2015<\/span><\/strong>, 54<\/span> (1):38-46. <\/span>[DOI<\/a>]<\/p>\n

2014<\/h3>\n

37. Hu W, Song H, Sae Her A, Bak DW, Naowarojna N, Elliott SJ, Qin L, Chen X, Liu P,
\n\u201cBioinformatic and Biochemical Characterizations of C-S Bond Formation and Cleavage Enzymes in the Fungus Neurospora crassa <\/span><\/em>Ergothioneine Biosynthetic\u00a0 Pathway,\u201d Organic Letter<\/span><\/em>, 2014<\/span><\/strong>, 16<\/span><\/em>(20): 5382-5385. [DOI<\/a>]<\/p>\n

36. Judd ET,\u00a0 Stein N, Pacheco AA, Elliott SJ, \u201cHydrogen Bonding Networks Tune Proton-Coupled
\nRedox Steps During the Enzymatic Six-electron Conversion of Nitrite to Ammonia,\u201d Biochemistry<\/span><\/em>, 2014<\/span><\/strong>, 53 <\/span><\/em>(35): 5638-5646. [DOI<\/a>]<\/p>\n

35. Funk MA, Judd ET, Marsh ENG, Elliott SJ, Drennan CL, \u201cStructures of benzylsuccinate synthase
\nelucidate roles of accessory subunits in glycyl radical enzyme activation and activity,\u201d Proc. Natl. Acad. Sci.<\/em> , 2014<\/span><\/strong>, 111<\/span><\/em>(28): 10161-10166. [DOI<\/a>]<\/p>\n

34. Bak DW and Elliott SJ, \u201cAlternative FeS cluster ligands: tuning redox potentials and chemistry,\u201d Current Opinions in Chemical Biology<\/em>, 2014<\/span><\/strong>, 19<\/em>: 50-58. [DOI<\/a>]<\/p>\n

2013<\/h3>\n

33. <\/span>Bak DW and Elliott SJ, \u201cConserved hydrogen bond networks tune FeS cluster binding and structural stability,\u201d Biochemistry<\/em>, <\/span>2013<\/span>, 52(27): 4687-4696. [<\/span>PDF<\/a>]<\/span><\/p>\n

32. Duncan GGM, Marritt SJ, Firer-Sherwood MA, Shi L, Richardson DJ, Evans SD, Elliott SJ<\/span>,
\nButt JN, Jeuken LJC. \u201cProtein-Protein Interaction Regulates the Direction of Catalysis and Electron Transfer in a Redox Enzyme Complex,\u201d J. Am. Chem. Soc.<\/span><\/em>, 2013<\/span><\/strong>,135<\/span> (28):10550-10556. [DOI<\/a>]<\/p>\n

31. Bewley KD, Ellis KE, Firer-Sherwood MA, Elliott SJ<\/span>. \u201cMulti-heme proteins: Nature\u2019s electronic multi-purpose tool,\u201d Biochimica et Biophysica Acta – Bioenergetics<\/span><\/em>, 2013<\/span><\/strong>, 1827<\/span><\/em> (8-9): 938-94. [DOI<\/a>]<\/p>\n

2012<\/h3>\n

30. <\/span> Judd ET, Youngblut M, Pacecho AA, <\/span>Elliott SJ<\/span>. \u201cDirect electrochemistry of Shewanella oneidensis cytochrome c nitrite reductase: evidence for interactions across the dimeric interface,\u201d <\/span>Biochemistry<\/span><\/em>, <\/span>2012<\/strong>, <\/span>51<\/span><\/em> (51):10175-85. [<\/span>PDF<\/a>]
\n<\/span><\/p>\n

29. Ellis KE, Frato KE, <\/span>Elliott SJ<\/span>. \u201cImpact of Quarternary Structure upon Bacterial Cytochrome c Peroxidases: does homodimerization matter?\u201d <\/span>Biochemistry<\/span><\/em>, <\/span>2012<\/span><\/strong>, <\/span>51<\/span><\/em>(50): 10008-10016. [<\/span>PDF<\/a>]
\n<\/span><\/p>\n

28. Hamill MJ, Jost M, Wong C, Bene NC*, Drennan CL, <\/span>Elliott SJ.<\/span> \u201cElectrochemical characterization of <\/span>Escherichia<\/span> <\/span>coli<\/span><\/em> adaptive response protein AidB\u201d, <\/span>International<\/em><\/span> <\/span>Journal<\/span> of <\/span>Molecular<\/span> <\/span>Sciences<\/span><\/em>, <\/span>2012<\/span><\/strong>, 13<\/em>(12), 16899-16915. [<\/span>DOI<\/a>]
\n<\/span><\/p>\n

27. Bewley KD, Firer-Sherwood MA, Mock JY*, Ando N, Drennan CL, <\/span>Elliott SJ<\/span>. \u201cMind the gap: diversity and reactivity of multiheme cytochromes of the MtrA\/DmsE family,\u201d <\/span>Transactions<\/span> <\/span>of<\/span> <\/span>the<\/span> <\/span>Biochemical<\/span> <\/span>Society<\/span><\/em>, <\/span>2012<\/span><\/strong>, 40<\/em>(6), 1268-1273. [<\/span>DOI<\/a>]
\n<\/span><\/p>\n

26. Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, <\/span>Elliott SJ<\/span>, Drennan CL. \u201cUnusual Role for a Mobile Flavin in a StaC-like Indolocarbazole Biosynthetic Enzyme,\u201d <\/span>Chemistry<\/span> <\/span>&<\/span> <\/span>Biology<\/span>, <\/span><\/em>2012<\/span><\/strong>, 19<\/em>(7), 855-865. [<\/span>DOI<\/a>]
\n<\/span><\/p>\n

25. Seidel J, Hoffmann M, Ellis KE, Seidel A, Spatzal T, Gerhardt S, <\/span>Elliott SJ<\/span>, Einsle O. \u201cMacA is a Second Cytochrome c Peroxidase of Geobacter sulfurreducens<\/em>\u201d, <\/span>Biochemistry<\/span>, <\/span>2012<\/span>, 50(21), 4513-20. [<\/span>PDF<\/a>]
\n<\/span><\/p>\n

24. Youngblut M, Judd EJ, Srajer V, Sayyed B, Groelzer T, <\/span>Elliott SJ<\/span>, Schmidt M, Pacheco AA. \u201cLaue crystal structure of Shewanella oneidensis<\/em> cytochrome c nitrite reductase from a high-yield expression system\u201d, <\/span>Journal<\/span> <\/span>of<\/span> <\/span>Biological<\/span> <\/span>Inorganic<\/span> <\/span>Chemistry<\/span><\/em>, <\/span>2012<\/span><\/strong>, 17<\/em>(4), 674-662. [<\/span>PDF<\/a>]<\/span>
\n<\/span><\/p>\n

23. Pulcu GS,\u00a0 Frato KE, Gupta R, Hsu H.-R., Levine GA, Hendrich MP, Elliott SJ. \u201cThe Cytochrome c <\/span>Peroxidase from Shewanella oneidensis<\/span><\/em> Requires Reductive Activation,\u201d Biochemistry<\/em>, <\/span>2012<\/span><\/strong>, 52<\/em>: 974-985. <\/span>[ PDF<\/a> ]<\/p>\n

2011<\/h3>\n

22. Hamill, M.J.; Jost, M.; Wong, C.Y.; Elliott, S.J.; Drennan, C.L. \u201cFlavin Induced Oligomerization in Escherichia coli<\/span><\/em> Adaptive Response Protein AidB,\u201d Biochemistry<\/span>, 2011<\/span>, 51: 10159-10169. [ PDF<\/a> ]<\/p>\n

21. Levin, B.D.; Can, M.; Bren, K.L.; Elliott, S.J. \u201cMethionine Lability in Bacterial Monoheme Cytochromes c<\/span>: an electrochemical study,\u201d Journal of Physical Chemistry – B<\/span>, 2011<\/span>, 11718-11726. [ PDF<\/a> ]<\/p>\n

20. Firer-Sherwood, M.A.; Ando, N.; Drennan, C.L.; Elliott, S.J. \u201cSolution-based Structural
\nAnalysis of the Decaheme Cytochrome MtrA, by Small Angle X-Ray Scattering and Analytical Ultracentrifugation,\u201d J. Phys. Chem.\u00a0 <\/span>– B, <\/span>2011<\/span>, 11208-1114. [PDF<\/a>]<\/p>\n

19. Ellis, K.E.; Seidel, J.; Einsle, O.; Elliott, S.J. \u201cGeobacter sulfurreducens<\/span><\/em> Cytochrome c<\/span> Peroxidases: electrochemical classification of catalytic mechanisms,\u201d Biochemistry<\/span>, 2011<\/span>, 51: 4513-4520. [PDF<\/a>]<\/p>\n

18. Firer-Sherwood, M.A.; Bewley, K.D.; Mock, J.Y.; Elliott, S.J. \u201cTools for Resolving Complexity in the Electron Transfer Networks of Multiheme Cytochromes\u201d Metallomics<\/span>, 2011<\/span>, 3:344-348. [PDF<\/a>]<\/p>\n

2010<\/h3>\n

17. Cong, H.; Becker, C.F.; Elliott, S.J.; Grinstaff, M.W.; Porco, J.A. \u201cSilver Nanoparticle-Catalyzed Diels-Alder Cycloadditions of 2\u2019-Hydroxychalcones\u201d. J. Am. Chem. Soc. <\/span>2010<\/span>, 132:7514-7518. [PDF<\/a>]<\/p>\n

2009<\/h3>\n

16. Bak, D.W.; Zuris, J.A.; Paddock, M.; Jennings, P.A.; Elliott, S.J.\u00a0 \u201cRedox Characterization of the FeS Protein MitoNEET and impact of thiazolidinedione drug binding.\u201d Biochemistry <\/span>2009<\/span>, 48(43):10193-5. [PDF<\/a>]<\/p>\n

15.\u00a0 Mitra, S.; Elliott, S.J. “Oxidative Disassembly of the [2Fe-2S] Cluster of Human Glutaredoxin 2 and Redox Regulation in the Mitochrondria.” Biochemistry<\/span> 2009<\/span>, 48(18):3813-3815. [PDF<\/a>]<\/p>\n

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.<\/span>” Biochemistry<\/span> 2009<\/span>, 48(1):87-95.[PDF<\/a>]<\/p>\n

2008<\/h3>\n

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<\/span> 2008<\/span>, 47(37):9738-9746. [PDF<\/a>]<\/p>\n

12. Hernandez, H.H.; Jaquez, O.; Hamill, M.J.; Elliott, S.J.; Drennan, C.L.\u00a0 “Thioredoxin reductase from Thermoplasma acidophilum<\/span><\/em>: a new twist on redox regulation” Biochemistry<\/span> 2008<\/span>, 47(37):9728-9737. [PDF<\/a>]<\/p>\n

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

10. Ye, T.; Kaur, R.; Senguen, F.T.; Michel, L.V.; Bren, K.L.; Elliott, S.J.\u00a0 “Methionine ligand lability of type I cytochromes c: detection of ligand loss using protein film voltammetry.” J. Am. Chem. Soc. <\/span>2008<\/span> 130(21):6682-3. [PDF<\/a>]<\/p>\n

2007<\/h3>\n

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

8.\u00a0 Ryan, K.S.; Howard-Jones, A.R.; Hamill, M.J.; Elliott, S.J.; Walsh, C.T.; Drennan, C.L.
\n“Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC.” Proc. Natl. Acad. Sci. USA<\/span> 2007<\/span> 104(39), 15311-6. [PDF<\/a>]<\/p>\n

7. Chobot, S.E.; Hernandez, H.H.; Drennan, C.L.; Elliott, S.J.\u00a0 “Direct Electrochemical Characterization of Archaeal Thioredoxins.” Angew. Chemie<\/span> 2007<\/span>, 46(22), 4145-7.<\/p>\n

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<\/span><\/em>: Redox cooperativity and conformational gating” J. Am. Chem. Soc.<\/span> 2007<\/span>, 129(7),1838-9. [PDF<\/a>]<\/p>\n

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

2006<\/h3>\n

4. Tarasev, M.; Pinto, A.; Kim, D.; Elliott, S.J.; Ballou, D.P.\u00a0 “The ‘bridging’ aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron (II)-mononuclear
\ncenter”. Biochemistry<\/span> 2006<\/span>, 45(34): 10208-16. [PDF<\/a>]<\/p>\n

2005<\/h3>\n

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<\/span>. 2005<\/span>, 44(24): 8999-9006. [PDF<\/a>]<\/p>\n

2. di Bernardo, D.; Thompson, M.J.; Gardner, T.S.; Chobot, S.E.*; Eastwood, E.L.; Wojtovich,
\nA.P.; Elliott, S.J.; Schaus, S.E.; Collins, J.J.\u00a0 “Chemogenomic Profiling on a Genome-wide Scale Using Reverse-Engineered Gene Networks”. Nature-Biotechnology<\/span>, 2005<\/span>, 23(3), 377-83.<\/p>\n

2004<\/h3>\n

1. Bradley, A.L.; Chobot, S.E.; Arciero, D.M.; Hooper, A.B.; Elliott, S.J..
\n“A Distinctive Electrocatalytic Response from the Cytochrome c Peroxidase of Nitrosomonas europaea<\/span><\/em>“. J. Biol. Chem.<\/span> 2004<\/span>, 279(14): 13297-13300. [ PDF<\/a>]
\n<\/span><\/p>\n","protected":false},"excerpt":{"rendered":"

2020 63. Zhu W, Walker LM, Tao L, Iavarone AT, Wei X, Britt RD, Elliott SJ, Klinman J, \u201cStructural Properties and Catalytic Implications of the SPASM Domain Iron\u2013Sulfur 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. […]<\/p>\n","protected":false},"author":11299,"featured_media":0,"parent":0,"menu_order":4,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/pages\/47"}],"collection":[{"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/users\/11299"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/comments?post=47"}],"version-history":[{"count":10,"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/pages\/47\/revisions"}],"predecessor-version":[{"id":277,"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/pages\/47\/revisions\/277"}],"wp:attachment":[{"href":"https:\/\/sites.bu.edu\/sje-lab\/wp-json\/wp\/v2\/media?parent=47"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}