| Year |
Citation |
Score |
| 2023 |
Dreishpoon MB, Bick NR, Petrova B, Warui DM, Cameron A, Booker SJ, Kanarek N, Golub TR, Tsvetkov P. FDX1 regulates cellular protein lipoylation through direct binding to LIAS. The Journal of Biological Chemistry. 105046. PMID 37453661 DOI: 10.1016/j.jbc.2023.105046 |
0.322 |
|
| 2023 |
Dreishpoon MB, Bick NR, Petrova B, Warui DM, Cameron A, Booker SJ, Kanarek N, Golub TR, Tsvetkov P. FDX1 regulates cellular protein lipoylation through direct binding to LIAS. Biorxiv : the Preprint Server For Biology. PMID 36778498 DOI: 10.1101/2023.02.03.526472 |
0.316 |
|
| 2022 |
Warui DM, Sil D, Lee KH, Neti SS, Esakova OA, Knox HL, Krebs C, Booker SJ. In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. Acs Bio & Med Chem Au. 2: 456-468. PMID 36281303 DOI: 10.1021/acsbiomedchemau.2c00020 |
0.438 |
|
| 2022 |
Neti SS, Sil D, Warui DM, Esakova OA, Solinski AE, Serrano DA, Krebs C, Booker SJ. Characterization of LipS1 and LipS2 from : Proteins Annotated as Biotin Synthases, which Together Catalyze Formation of the Lipoyl Cofactor. Acs Bio & Med Chem Au. 2: 509-520. PMID 36281299 DOI: 10.1021/acsbiomedchemau.2c00018 |
0.466 |
|
| 2022 |
Schulz V, Basu S, Freibert SA, Webert H, Boss L, Mühlenhoff U, Pierrel F, Essen LO, Warui DM, Booker SJ, Stehling O, Lill R. Functional spectrum and specificity of mitochondrial ferredoxins FDX1 and FDX2. Nature Chemical Biology. PMID 36280795 DOI: 10.1038/s41589-022-01159-4 |
0.312 |
|
| 2022 |
Knox HL, Booker SJ. Structural characterization of cobalamin-dependent radical S-adenosylmethionine methylases. Methods in Enzymology. 669: 3-27. PMID 35644177 DOI: 10.1016/bs.mie.2021.12.013 |
0.423 |
|
| 2022 |
Booker S. The biosynthesis of lipoic acid: A saga of death, destruction, and rebirth. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35553478 DOI: 10.1096/fasebj.2022.36.S1.0I186 |
0.484 |
|
| 2022 |
Wang B, Silakov A, Booker SJ. Using peptide substrate analogs to characterize a radical intermediate in NosN catalysis. Methods in Enzymology. 666: 469-487. PMID 35465928 DOI: 10.1016/bs.mie.2022.02.008 |
0.323 |
|
| 2022 |
Pagnier A, Balci B, Shepard EM, Yang H, Warui DM, Impano S, Booker SJ, Hoffman BM, Broderick WE, Broderick JB. [FeFe]-Hydrogenase: Defined Lysate-Free Maturation Reveals a Key Role for Lipoyl-H-Protein in DTMA Ligand Biosynthesis. Angewandte Chemie (International Ed. in English). PMID 35319808 DOI: 10.1002/anie.202203413 |
0.666 |
|
| 2022 |
Knox HL, Sinner EK, Townsend CA, Boal AK, Booker SJ. Structure of a B-dependent radical SAM enzyme in carbapenem biosynthesis. Nature. 602: 343-348. PMID 35110734 DOI: 10.1038/s41586-021-04392-4 |
0.31 |
|
| 2021 |
Esakova OA, Grove TL, Yennawar NH, Arcinas AJ, Wang B, Krebs C, Almo SC, Booker SJ. Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB. Nature. PMID 34526715 DOI: 10.1038/s41586-021-03904-6 |
0.393 |
|
| 2021 |
Jeyachandran VR, Pendyala JV, McCarthy EL, Boal AK, Booker SJ. Biochemical Approaches to Probe the Role of the Auxiliary Iron-Sulfur Cluster of Lipoyl Synthase from Mycobacterium Tuberculosis. Methods in Molecular Biology (Clifton, N.J.). 2353: 307-332. PMID 34292556 DOI: 10.1007/978-1-0716-1605-5_16 |
0.459 |
|
| 2021 |
Knox HL, Chen PY, Blaszczyk AJ, Mukherjee A, Grove TL, Schwalm EL, Wang B, Drennan CL, Booker SJ. Structural basis for non-radical catalysis by TsrM, a radical SAM methylase. Nature Chemical Biology. PMID 33462497 DOI: 10.1038/s41589-020-00717-y |
0.42 |
|
| 2020 |
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 |
0.469 |
|
| 2020 |
Knox HL, Chen PY, Blaszczyk AJ, Grove TL, Schwalm EL, Wang B, Drennan CL, Booker SJ. Crystallographic snapshots of TsrM, a radical S‐adenosylmethionine enzyme whose reaction is not so radical The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.00561 |
0.393 |
|
| 2019 |
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 |
0.461 |
|
| 2019 |
Blaszczyk AJ, Knox HL, Booker SJ. Understanding the role of electron donors in the reaction catalyzed by Tsrm, a cobalamin-dependent radical S-adenosylmethionine methylase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31350635 DOI: 10.1007/S00775-019-01689-8 |
0.478 |
|
| 2019 |
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 |
0.422 |
|
| 2019 |
Radle MI, Miller DV, Laremore TN, Booker SJ. Methanogenesis marker protein 10 (Mmp10) from is a radical -adenosylmethionine methylase that unexpectedly requires cobalamin. The Journal of Biological Chemistry. PMID 31113866 DOI: 10.1074/Jbc.Ra119.007609 |
0.379 |
|
| 2019 |
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 |
0.469 |
|
| 2018 |
McCarthy EL, Rankin AN, Dill ZR, Booker SJ. The A-type domain in NfuA is required for regenerating the auxiliary [4Fe-4S] cluster in lipoyl synthase. The Journal of Biological Chemistry. PMID 30538130 DOI: 10.1074/Jbc.Ra118.006171 |
0.458 |
|
| 2018 |
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 |
0.771 |
|
| 2018 |
Maiocco SJ, Arcinas AJ, Booker SJ, Elliott SJ. Parsing Redox Potentials of the Five Ferredoxins found within Thermotoga maritima. Protein Science : a Publication of the Protein Society. PMID 30418685 DOI: 10.1002/Pro.3547 |
0.496 |
|
| 2018 |
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 : a Publication of the Protein Society. PMID 30394621 DOI: 10.1002/Pro.3548 |
0.523 |
|
| 2018 |
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 |
0.415 |
|
| 2018 |
McCarthy EL, Booker SJ. Biochemical Approaches for Understanding Iron-Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis. Methods in Enzymology. 606: 217-239. PMID 30097094 DOI: 10.1016/Bs.Mie.2018.06.006 |
0.539 |
|
| 2018 |
Holliday GL, Akiva E, Meng EC, Brown SD, Calhoun S, Pieper U, Sali A, Booker SJ, Babbitt PC. Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a "Plug and Play" Domain. Methods in Enzymology. 606: 1-71. PMID 30097089 DOI: 10.1016/Bs.Mie.2018.06.004 |
0.366 |
|
| 2018 |
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 |
0.47 |
|
| 2018 |
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 |
0.438 |
|
| 2018 |
Blaszczyk AJ, Booker SJ. A (Re)Discovery of the Fom3 Substrate. Biochemistry. PMID 29345912 DOI: 10.1021/Acs.Biochem.7B01281 |
0.305 |
|
| 2018 |
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 |
0.467 |
|
| 2017 |
McCarthy EL, Booker SJ. Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase. Science (New York, N.Y.). 358: 373-377. PMID 29051382 DOI: 10.1126/Science.Aan4574 |
0.506 |
|
| 2017 |
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 |
0.472 |
|
| 2017 |
Blaszczyk AJ, Wang RX, Booker SJ. TsrM as a Model for Purifying and Characterizing Cobalamin-Dependent Radical S-Adenosylmethionine Methylases. Methods in Enzymology. 595: 303-329. PMID 28882204 DOI: 10.1016/Bs.Mie.2017.07.007 |
0.543 |
|
| 2017 |
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 |
0.491 |
|
| 2017 |
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 |
0.465 |
|
| 2017 |
Yennawar N, Esakova O, Grove T, Silakov A, Saunders A, McLaughlin M, Booker S. A structural study of quinolinate synthase, a key enzyme in bacterial NAD+ biosynthesis Acta Crystallographica Section a Foundations and Advances. 73: a150-a150. DOI: 10.1107/S0108767317098518 |
0.782 |
|
| 2016 |
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 |
0.485 |
|
| 2016 |
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 |
0.509 |
|
| 2016 |
Block E, Booker S, Flores-Penalba S, George G, Gundala S, Landgraf B, Liu J, Lodge S, Pushie J, Rozovsky S, Vattekkatte A, Yaghi R, Zeng H. Trifluoroselenomethionine - a New Non-Natural Amino Acid. Chembiochem : a European Journal of Chemical Biology. PMID 27383291 DOI: 10.1002/Cbic.201600266 |
0.423 |
|
| 2016 |
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 |
0.818 |
|
| 2016 |
Landgraf BJ, McCarthy EL, Booker SJ. Radical S-Adenosylmethionine Enzymes in Human Health and Disease. Annual Review of Biochemistry. PMID 27145839 DOI: 10.1146/Annurev-Biochem-060713-035504 |
0.433 |
|
| 2016 |
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 |
0.34 |
|
| 2016 |
Landgraf BJ, Booker SJ. The Stereochemical Course of the Reaction Catalyzed by RimO, a Radical SAM Methylthiotransferase. Journal of the American Chemical Society. PMID 26871608 DOI: 10.1021/Jacs.5B11035 |
0.493 |
|
| 2016 |
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 |
0.535 |
|
| 2016 |
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 |
0.796 |
|
| 2015 |
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 |
0.531 |
|
| 2015 |
McCarthy EL, Booker SJ. Bridging a gap in iron-sulfur cluster assembly. Elife. 4. PMID 26350572 DOI: 10.7554/Elife.10479 |
0.391 |
|
| 2015 |
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 |
0.674 |
|
| 2015 |
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 |
0.461 |
|
| 2015 |
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 |
0.502 |
|
| 2015 |
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 |
0.536 |
|
| 2015 |
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 |
0.424 |
|
| 2015 |
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 |
0.653 |
|
| 2015 |
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 |
0.388 |
|
| 2014 |
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 |
0.528 |
|
| 2014 |
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 |
0.465 |
|
| 2013 |
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 |
0.498 |
|
| 2013 |
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 |
0.532 |
|
| 2013 |
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 |
0.657 |
|
| 2013 |
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 |
0.353 |
|
| 2013 |
Landgraf BJ, Booker SJ. Biochemistry: The ylide has landed. Nature. 498: 45-7. PMID 23676671 DOI: 10.1038/Nature12247 |
0.417 |
|
| 2013 |
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 |
0.527 |
|
| 2013 |
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 |
0.418 |
|
| 2013 |
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 |
0.572 |
|
| 2013 |
Maiocco SJ, Grove T, Goldman P, Booker S, Drennan C, Elliott S. Electrochemical investigation of a radical sadenosylmethionine enzyme: BtrN from Bacillus circulans The Faseb Journal. 27. DOI: 10.1096/Fasebj.27.1_Supplement.Lb57 |
0.401 |
|
| 2013 |
Maiocco SJ, Grove T, Sites L, Booker SJ, Elliott SJ. Electrochemical Investigation of the Radical SAM Enzyme, BtrN from Bacillus Circulans Biophysical Journal. 104: 489a. DOI: 10.1016/J.Bpj.2012.11.2698 |
0.502 |
|
| 2012 |
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 |
0.52 |
|
| 2012 |
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 |
0.592 |
|
| 2012 |
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 |
0.385 |
|
| 2012 |
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 |
0.531 |
|
| 2011 |
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 |
0.533 |
|
| 2011 |
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 |
0.434 |
|
| 2011 |
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 |
0.634 |
|
| 2011 |
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 |
0.676 |
|
| 2011 |
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 |
0.387 |
|
| 2011 |
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 |
0.658 |
|
| 2011 |
Arcinas AJ, Booker SJ. Enzymology: Radical break-up, blissful make-up. Nature Chemical Biology. 7: 133-4. PMID 21321550 DOI: 10.1038/Nchembio.528 |
0.387 |
|
| 2010 |
Booker SJ, Grove TL. Mechanistic and functional versatility of radical SAM enzymes. F1000 Biology Reports. 2: 52. PMID 21152342 DOI: 10.3410/B2-52 |
0.449 |
|
| 2010 |
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 |
0.48 |
|
| 2010 |
Billgren ES, Cicchillo RM, Nesbitt NM, Booker SJ. Lipoic acid biosynthesis and enzymology Comprehensive Natural Products Ii: Chemistry and Biology. 7: 181-212. |
0.756 |
|
| 2009 |
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 |
0.682 |
|
| 2009 |
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 |
0.56 |
|
| 2009 |
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 |
0.489 |
|
| 2008 |
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 |
0.465 |
|
| 2008 |
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 |
0.797 |
|
| 2008 |
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 |
0.821 |
|
| 2008 |
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 |
0.554 |
|
| 2007 |
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 |
0.778 |
|
| 2007 |
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 |
0.443 |
|
| 2005 |
Iwig DF, Uchida A, Stromberg JA, Booker SJ. The activity of Escherichia coli cyclopropane fatty acid synthase depends on the presence of bicarbonate. Journal of the American Chemical Society. 127: 11612-3. PMID 16104732 DOI: 10.1021/Ja053899Z |
0.476 |
|
| 2005 |
Cicchillo RM, Tu L, Stromberg JA, Hoffart LM, Krebs C, Booker SJ. Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. Journal of the American Chemical Society. 127: 7310-1. PMID 15898769 DOI: 10.1021/Ja051369X |
0.807 |
|
| 2005 |
Cicchillo RM, Booker SJ. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. Journal of the American Chemical Society. 127: 2860-1. PMID 15740115 DOI: 10.1021/Ja042428U |
0.759 |
|
| 2005 |
Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ. Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. Protein Expression and Purification. 39: 269-82. PMID 15642479 DOI: 10.1016/J.Pep.2004.10.021 |
0.803 |
|
| 2004 |
Iwig DF, Grippe AT, McIntyre TA, Booker SJ. Isotope and elemental effects indicate a rate-limiting methyl transfer as the initial step in the reaction catalyzed by Escherichia coli cyclopropane fatty acid synthase. Biochemistry. 43: 13510-24. PMID 15491158 DOI: 10.1021/Bi048692H |
0.45 |
|
| 2004 |
Iwig DF, Booker SJ. Insight into the polar reactivity of the onium chalcogen analogues of S-adenosyl-L-methionine. Biochemistry. 43: 13496-509. PMID 15491157 DOI: 10.1021/Bi048693+ |
0.33 |
|
| 2004 |
Cicchillo RM, Lee KH, Baleanu-Gogonea C, Nesbitt NM, Krebs C, Booker SJ. Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry. 43: 11770-81. PMID 15362861 DOI: 10.1021/Bi0488505 |
0.809 |
|
| 2004 |
Cicchillo RM, Iwig DF, Jones AD, Nesbitt NM, Baleanu-Gogonea C, Souder MG, Tu L, Booker SJ. Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid. Biochemistry. 43: 6378-86. PMID 15157071 DOI: 10.1021/Bi049528X |
0.809 |
|
| 2004 |
Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, Booker SJ. Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. The Journal of Biological Chemistry. 279: 32418-25. PMID 15155761 DOI: 10.1074/Jbc.M404381200 |
0.79 |
|
| 2004 |
Booker SJ. Unraveling the pathway of lipoic acid biosynthesis. Chemistry & Biology. 11: 10-2. PMID 15112987 DOI: 10.1016/J.Chembiol.2004.01.002 |
0.368 |
|
| 2001 |
Frey PA, Booker SJ. Radical mechanisms of S-adenosylmethionine-dependent enzymes. Advances in Protein Chemistry. 58: 1-45. PMID 11665486 DOI: 10.1016/S0065-3233(01)58001-8 |
0.638 |
|
| 2000 |
Cosper NJ, Booker SJ, Ruzicka F, Frey PA, Scott RA. Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase. Biochemistry. 39: 15668-73. PMID 11123891 DOI: 10.1021/Bi0022184 |
0.644 |
|
| 2000 |
Wu W, Booker S, Lieder KW, Bandarian V, Reed GH, Frey PA. Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism. Biochemistry. 39: 9561-70. PMID 10924153 DOI: 10.1021/Bi000658P |
0.659 |
|
| 1999 |
Licht SS, Booker S, Stubbe J. Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation. Biochemistry. 38: 1221-33. PMID 9930982 DOI: 10.1021/Bi981885I |
0.687 |
|
| 1998 |
Lieder KW, Booker S, Ruzicka FJ, Beinert H, Reed GH, Frey PA. S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance. Biochemistry. 37: 2578-85. PMID 9485408 DOI: 10.1021/Bi972417W |
0.669 |
|
| 1996 |
Sari MA, Booker S, Jaouen M, Vadon S, Boucher JI, Pompon D, Mansuy D. Expression in yeast and purification of functional macrophage nitric oxide synthase. Evidence for cysteine-194 as iron proximal ligand. Biochemistry. 35: 7204-13. PMID 8679549 DOI: 10.1021/Bi960087U |
0.449 |
|
| 1994 |
Booker S, Licht S, Broderick J, Stubbe J. Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction. Biochemistry. 33: 12676-85. PMID 7918494 DOI: 10.1021/Bi00208A019 |
0.782 |
|
| 1993 |
Booker S, Stubbe J. Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii Proceedings of the National Academy of Sciences of the United States of America. 90: 8352-8356. PMID 8397403 DOI: 10.1073/Pnas.90.18.8352 |
0.594 |
|
| 1993 |
Booker S, Broderick J, Stubbe J. Ribonucleotide reductases: Radical enzymes with suicidal tendencies Biochemical Society Transactions. 21: 727-730. PMID 8224499 DOI: 10.1042/Bst0210727 |
0.729 |
|
| 1992 |
Mao SS, Holler TP, Yu GX, Bollinger JM, Booker S, Johnston MI, Stubbe J. A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing. Biochemistry. 31: 9733-43. PMID 1382592 |
0.55 |
|
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