User talk:Guacamole21/Squire Booker

This article does not have much about Squire Booker. To improve the article, there needs to be sections developed which discuss his education, career, research which includes thorough explanations with diagrams, and publications. Images and diagrams need to be added. There needs to be better and more resources listed. Guacamole21 (talk) 02:32, 14 January 2020 (UTC)

Some sources for the bibliography include:

1. Bandarian, V. Radical SAM enzymes; Academic Press, an imprint of Elsevier: Cambridge MA, 2018.

2. Zhang B, Arcinas AJ, Radle MI, Silakov A, Booker SJ, Krebs C. The First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]0-like Auxiliary Cluster. Journal of the American Chemical Society. PMID 31899624 DOI: 10.1021/jacs.9b11093

3. Esakova OA, Silakov A, Grove TL, Warui DM, Yennawar NH, Booker SJ. An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase. Journal of the American Chemical Society. PMID 31390192 DOI: 10.1021/jacs.9b02513

4. Gumkowski JD, Martinie RJ, Corrigan P, Pan J, Bauerle MR, Almarei M, Booker SJ, Silakov A, Krebs C, Boal AK. Analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an iron-binding accessory domain in a clostridial enzyme. Biochemistry. PMID 31246421 DOI: 10.1021/acs.biochem.9b00197

5. Wang B, LaMattina JW, Marshall S, Booker SJ. Capturing Intermediates in the Reaction Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side Ring System. Journal of the American Chemical Society. PMID 30865439 DOI: 10.1021/jacs.8b13157

6. Ronnebaum TA, McFarlane JS, Prisinzano TE, Booker SJ, Lamb AL. Stuffed Methyltransferase Catalyzes Penultimate Step of Pyochelin Biosynthesis. Biochemistry. PMID 30525512 DOI: 10.1021/acs.biochem.8b00716

7. Wang B, LaMattina JW, Badding ED, Gadsby LK, Grove TL, Booker SJ. Using Peptide Mimics to Study the Biosynthesis of the Side-Ring System of Nosiheptide. Methods in Enzymology. 606: 241-268. PMID 30097095 DOI: 10.1016/bs.mie.2018.06.005

8. Wang B, Blaszczyk AJ, Knox H, Zhou S, Blaesi EJ, Krebs C, Wang R, Booker SJ. Stereochemical and Mechanistic Investigation of the Reaction Catalyzed by Fom3 from Streptomyces fradiae, a Cobalamin-Dependent Radical S-Adenosylmethionine Methylase. Biochemistry. PMID 30036047 DOI: 10.1021/acs.biochem.8b00693

9. Bauerle MR, Grove TL, Booker SJ. Investigation of Solvent Hydron Exchange in the Reaction Catalyzed by the Antibiotic Resistance Protein, Cfr. Biochemistry. PMID 29787246 DOI: 10.1021/acs.biochem.8b00347

10. Lanz N, Blaszczyk AJ, McCarthy E, Wang B, Wang R, Jones B, Booker SJ. Enhanced Solubilization of Class B Radical S-adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia coli. Biochemistry. PMID 29298049 DOI: 10.1021/acs.biochem.7b01205

11. LaMattina JW, Wang B, Badding ED, Gadsby LK, Grove T, Booker SJ. The Radical S-Adenosylmethionine Methylase NosN Catalyzes both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide. Journal of the American Chemical Society. PMID 29039940 DOI: 10.1021/jacs.7b08492

12. Blaszczyk AJ, Wang B, Silakov A, Ho JV, Booker SJ. Efficient Methylation of C2 in L-Tryptophan by the Cobalamin-dependent Radical S-Adenosylmethionine Methylase TsrM Requires an Unmodified N1 Amine. The Journal of Biological Chemistry. PMID 28747433 DOI: 10.1074/jbc.M117.778548

13. Badding E, Grove TL, Gadsby L, LaMattina J, Boal AK, Booker SJ. Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK. Journal of the American Chemical Society. PMID 28343381 DOI: 10.1021/jacs.7b01497

14. 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. PMID 27598886 DOI: 10.1021/acs.biochem.6b00670

15. McLaughlin MI, Lanz ND, Goldman PJ, Lee KH, Booker SJ, Drennan CL. Crystallographic snapshots of sulfur insertion by lipoyl synthase. Proceedings of the National Academy of Sciences of the United States of America. PMID 27506792 DOI: 10.1073/pnas.1602486113

16. Esakova OA, Silakov A, Grove TL, Saunders AH, McLaughlin MI, Yennawar NH, Booker SJ. Structure of Quinolinate Synthase from Pyrococcus horikoshii in the Presence of Its Product, Quinolinic Acid. Journal of the American Chemical Society. PMID 27224840 DOI: 10.1021/jacs.6b02708

17. Schwalm EL, Grove TL, Booker SJ, Boal AK. Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA. Science (New York, N.Y.). 352: 309-12. PMID 27081063 DOI: 10.1126/science.aad5367

18. 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. Journal of the American Chemical Society. PMID 26841310 DOI: 10.1021/jacs.5b12592

19. Lanz ND, Lee KH, Horstmann AK, Pandelia ME, Cicchillo RM, Krebs C, Booker SJ. Characterization of Lipoyl Synthase from Mycobacterium tuberculosis. Biochemistry. PMID 26841001 DOI: 10.1021/acs.biochem.5b01216

20. Lanz ND, Rectenwald JM, Wang B, Kakar ES, Laremore TN, Booker SJ, Silakov A. Characterization of a Radical Intermediate in Lipoyl Cofactor Biosynthesis. Journal of the American Chemical Society. PMID 26390103 DOI: 10.1021/jacs.5b04387

21. McCarthy EL, Booker SJ. Bridging a gap in iron-sulfur cluster assembly. Elife. 4. PMID 26350572 DOI: 10.7554/eLife.10479

22. Rajakovich LJ, Nørgaard H, Warui DM, Chang WC, Li N, Booker SJ, Krebs C, Bollinger JM, Pandelia ME. Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism. Journal of the American Chemical Society. 137: 11695-709. PMID 26284355 DOI: 10.1021/jacs.5b06345

23. Marous DR, Lloyd EP, Buller AR, Moshos KA, Grove TL, Blaszczyk AJ, Booker SJ, Townsend CA. Consecutive radical S-adenosylmethionine methylations form the ethyl side chain in thienamycin biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 112: 10354-8. PMID 26240322 DOI: 10.1073/pnas.1508615112

24. 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. Journal of the American Chemical Society. PMID 26088836 DOI: 10.1021/jacs.5b03384

25. Lanz ND, Booker SJ. Auxiliary iron-sulfur cofactors in radical SAM enzymes. Biochimica Et Biophysica Acta. 1853: 1316-1334. PMID 25597998 DOI: 10.1016/j.bbamcr.2015.01.002

26. Pandelia ME, Lanz ND, Booker SJ, Krebs C. Mössbauer spectroscopy of Fe/S proteins. Biochimica Et Biophysica Acta. 1853: 1395-1405. PMID 25498248 DOI: 10.1016/j.bbamcr.2014.12.005

27. Warui DM, Pandelia ME, Rajakovich LJ, Krebs C, Bollinger JM, Booker SJ. Efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase. Biochemistry. 54: 1006-15. PMID 25496470 DOI: 10.1021/bi500847u

28. Bauerle MR, Schwalm EL, Booker SJ. Mechanistic diversity of radical S-adenosylmethionine (SAM)-dependent methylation. The Journal of Biological Chemistry. 290: 3995-4002. PMID 25477520 DOI: 10.1074/jbc.R114.607044

29. Lanz ND, Pandelia ME, Kakar ES, Lee KH, Krebs C, Booker SJ. Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase. Biochemistry. 53: 4557-72. PMID 24901788 DOI: 10.1021/bi500432r

30. Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. Journal of the American Chemical Society. 136: 8221-8. PMID 24806349 DOI: 10.1021/ja410560p

31. Goldman PJ, Grove TL, Booker SJ, Drennan CL. X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proceedings of the National Academy of Sciences of the United States of America. 110: 15949-54. PMID 24048029 DOI: 10.1073/pnas.1312228110

32. Landgraf BJ, Arcinas AJ, Lee KH, Booker SJ. Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB. Journal of the American Chemical Society. 135: 15404-16. PMID 23991893 DOI: 10.1021/ja4048448

33. Pandelia ME, Li N, Nørgaard H, Warui DM, Rajakovich LJ, Chang WC, Booker SJ, Krebs C, Bollinger JM. Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate. Journal of the American Chemical Society. 135: 15801-12. PMID 23987523 DOI: 10.1021/ja405047b

34. Christensen QH, Grove TL, Booker SJ, Greenberg EP. A high-throughput screen for quorum-sensing inhibitors that target acyl-homoserine lactone synthases. Proceedings of the National Academy of Sciences of the United States of America. 110: 13815-20. PMID 23924613 DOI: 10.1073/pnas.1313098110

35. Landgraf BJ, Booker SJ. Biochemistry: The ylide has landed. Nature. 498: 45-7. PMID 23676671 DOI: 10.1038/nature12247

36. Goldman PJ, Grove TL, Sites LA, McLaughlin MI, Booker SJ, Drennan CL. X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proceedings of the National Academy of Sciences of the United States of America. 110: 8519-24. PMID 23650368 DOI: 10.1073/pnas.1302417110

37. Grove TL, Livada J, Schwalm EL, Green MT, Booker SJ, Silakov A. A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr. Nature Chemical Biology. 9: 422-7. PMID 23644479 DOI: 10.1038/nchembio.1251

38. Grove TL, Ahlum JH, Qin RM, Lanz ND, Radle MI, Krebs C, Booker SJ. Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in the mechanism of catalysis. Biochemistry. 52: 2874-87. PMID 23477283 DOI: 10.1021/bi400136u

39. Lanz ND, Grove TL, Gogonea CB, Lee KH, Krebs C, Booker SJ. RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins. Methods in Enzymology. 516: 125-52. PMID 23034227 DOI: 10.1016/B978-0-12-394291-3.00030-7

40. Li N, Chang WC, Warui DM, Booker SJ, Krebs C, Bollinger JM. Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases. Biochemistry. 51: 7908-16. PMID 22947199 DOI: 10.1021/bi300912n

41. Booker SJ. Radical SAM enzymes and radical enzymology. Biochimica Et Biophysica Acta. 1824: 1151-3. PMID 22850428 DOI: 10.1016/j.bbapap.2012.07.006

42. Lanz ND, Booker SJ. Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes. Biochimica Et Biophysica Acta. 1824: 1196-212. PMID 22846545 DOI: 10.1016/j.bbapap.2012.07.009

43. Grove TL, Radle MI, Krebs C, Booker SJ. Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. Journal of the American Chemical Society. 133: 19586-9. PMID 21916495 DOI: 10.1021/ja207327v

44. Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC. Structural basis for methyl transfer by a radical SAM enzyme. Science (New York, N.Y.). 332: 1089-92. PMID 21527678 DOI: 10.1126/science.1205358

45. Li N, Nørgaard H, Warui DM, Booker SJ, Krebs C, Bollinger JM. Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase. Journal of the American Chemical Society. 133: 6158-61. PMID 21462983 DOI: 10.1021/ja2013517

46. Krebs C, Bollinger JM, Booker SJ. Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins. Current Opinion in Chemical Biology. 15: 291-303. PMID 21440485 DOI: 10.1016/j.cbpa.2011.02.019

47. Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science (New York, N.Y.). 332: 604-7. PMID 21415317 DOI: 10.1126/science.1200877

48. Warui DM, Li N, Nørgaard H, Krebs C, Bollinger JM, Booker SJ. Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase. Journal of the American Chemical Society. 133: 3316-9. PMID 21341652 DOI: 10.1021/ja111607x

49. Arcinas AJ, Booker SJ. Enzymology: Radical break-up, blissful make-up. Nature Chemical Biology. 7: 133-4. PMID 21321550 DOI: 10.1038/nchembio.528

50. Booker SJ, Grove TL. Mechanistic and functional versatility of radical SAM enzymes. F1000 Biology Reports. 2: 52. PMID 21152342 DOI: 10.3410/B2-52

51. Grove TL, Ahlum JH, Sharma P, Krebs C, Booker SJ. A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters. Biochemistry. 49: 3783-5. PMID 20377206 DOI: 10.1021/bi9022126

52. Billgren ES, Cicchillo RM, Nesbitt NM, Booker SJ. Lipoic acid biosynthesis and enzymology Comprehensive Natural Products Ii: Chemistry and Biology. 7: 181-212.

53. Matthews ML, Neumann CS, Miles LA, Grove TL, Booker SJ, Krebs C, Walsh CT, Bollinger JM. Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2. Proceedings of the National Academy of Sciences of the United States of America. 106: 17723-8. PMID 19815524 DOI: 10.1073/pnas.0909649106

54. Lee KH, Saleh L, Anton BP, Madinger CL, Benner JS, Iwig DF, Roberts RJ, Krebs C, Booker SJ. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry. 48: 10162-74. PMID 19736993 DOI: 10.1021/bi900939w

55. Booker SJ. Anaerobic functionalization of unactivated C-H bonds. Current Opinion in Chemical Biology. 13: 58-73. PMID 19297239 DOI: 10.1016/j.cbpa.2009.02.036

56. Chatterjee A, Li Y, Zhang Y, Grove TL, Lee M, Krebs C, Booker SJ, Begley TP, Ealick SE. Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily. Nature Chemical Biology. 4: 758-65. PMID 18953358 DOI: 10.1038/nchembio.121

57. Saunders AH, Griffiths AE, Lee KH, Cicchillo RM, Tu L, Stromberg JA, Krebs C, Booker SJ. Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes. Biochemistry. 47: 10999-1012. PMID 18803397 DOI: 10.1021/bi801268f

58. Saunders AH, Booker SJ. Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation. Biochemistry. 47: 8467-9. PMID 18651751 DOI: 10.1021/bi801135y

59. Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry. 47: 7523-38. PMID 18558715 DOI: 10.1021/bi8004297

60. Booker SJ, Cicchillo RM, Grove TL. Self-sacrifice in radical S-adenosylmethionine proteins. Current Opinion in Chemical Biology. 11: 543-52. PMID 17936058 DOI: 10.1016/j.cbpa.2007.08.028

61. van der Donk WA, Booker SJ. Never stop questioning Current Opinion in Chemical Biology. 11: 527-528. DOI: 10.1016/j.cbpa.2007.08.022

62. Welcome New Associate Editor, Squire Booker Alanna Schepartz Biochemistry 2019 58 (51), 5099-5099 DOI: 10.1021/acs.biochem.9b01057

63. https://chemistry.umbc.edu/dr-squire-j-booker/

64. http://news.mit.edu/2019/mit-alumnus-squire-booker-investiture-doctoral-hoods-speaker-0403

65. https://biochem.wisc.edu/news/2019/news-squire-booker-postdoc-alumnus-profile-2019-03-07

66. https://chemistry.mit.edu/chemistry-news/squire-booker-phd-94-elected-to-national-academy-of-sciences/ Guacamole21 (talk) 02:56, 14 January 2020 (UTC)