2019 - Member of the National Academy of Sciences
2017 - Fellow of the American Academy of Arts and Sciences
2013 - Fellow of the American Association for the Advancement of Science (AAAS)
Squire J. Booker mainly investigates Stereochemistry, Biochemistry, Radical SAM, Enzyme and ATP synthase. Squire J. Booker combines subjects such as Substrate, Lysine, Cofactor and Escherichia coli with his study of Stereochemistry. The various areas that he examines in his Cofactor study include Oxygenase, Bond cleavage and Peroxide.
His Biochemistry research focuses on Ribonucleotide, Cysteine and Biosynthesis. His Radical SAM study incorporates themes from Protein structure and Methylation. His studies in ATP synthase integrate themes in fields like Glycine, Cleavage and Sulfur.
Squire J. Booker mostly deals with Stereochemistry, Biochemistry, Enzyme, Cofactor and Radical SAM. His study explores the link between Stereochemistry and topics such as Biosynthesis that cross with problems in Ring. ATP synthase, Escherichia coli, Cysteine, Ribonucleotide and Active site are the subjects of his Biochemistry studies.
His Enzyme research integrates issues from Thermotoga maritima, Cleavage and Radical. His research integrates issues of Enzyme catalysis, Moiety, Indole test, Quinolinate and Redox in his study of Cofactor. Squire J. Booker has researched Radical SAM in several fields, including Residue and Iron–sulfur cluster.
Stereochemistry, Radical SAM, Cofactor, Enzyme and Biosynthesis are his primary areas of study. The study incorporates disciplines such as Methylation, Methyltransferase and Catalysis in addition to Stereochemistry. His Radical SAM study combines topics in areas such as Iron–sulfur cluster, Nucleophile and Escherichia coli.
His Cofactor study combines topics from a wide range of disciplines, such as Dihydroxyacetone phosphate, Residue, DHAP, Quinolinate and ATP synthase. His research in Enzyme intersects with topics in Crystallography and Regulation of gene expression. When carried out as part of a general Biochemistry research project, his work on Protein methylation and Complementation is frequently linked to work in Methanosarcina acetivorans, therefore connecting diverse disciplines of study.
Squire J. Booker mainly focuses on Radical SAM, Methylation, Methyltransferase, Biochemistry and Biosynthesis. His Radical SAM research includes themes of Divergent evolution, Biogenesis and Escherichia coli. The Protein methylation research Squire J. Booker does as part of his general Methyltransferase study is frequently linked to other disciplines of science, such as Methanosarcina acetivorans, therefore creating a link between diverse domains of science.
Squire J. Booker interconnects Bicyclic molecule, Stereochemistry, Cofactor and Peptide in the investigation of issues within Biosynthesis. His studies deal with areas such as Thioester and Ring as well as Stereochemistry. His Thermotoga maritima research extends to Enzyme, which is thematically connected.
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A Model for the Role of Multiple Cysteine Residues Involved in Ribonucleotide Reduction: Amazing and Still Confusing
S. S. Mao;T. P. Holler;G. X. Yu;J. M. Bollinger.
A Radically Different Mechanism for S-Adenosylmethionine–Dependent Methyltransferases
Tyler L. Grove;Jack S. Benner;Matthew I. Radle;Jessica H. Ahlum.
Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2
Megan L. Matthews;Christopher S. Neumann;Linde A. Miles;Tyler L. Grove.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid.
Robert M. Cicchillo;David F. Iwig;A. Daniel Jones;Natasha M. Nesbitt.
Mechanistic Diversity of Radical S-Adenosylmethionine (SAM)-dependent Methylation
Matthew R. Bauerle;Erica L. Schwalm;Squire J. Booker.
Journal of Biological Chemistry (2015)
Structural basis for methyl transfer by a radical SAM enzyme
Amie K. Boal;Tyler L. Grove;Monica I. McLaughlin;Neela H. Yennawar.
Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
Robert M. Cicchillo;Squire J. Booker.
Journal of the American Chemical Society (2005)
Escherichia coli Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide†
Robert M. Cicchillo;Kyung Hoon Lee;Camelia Baleanu-Gogonea;Natasha M. Nesbitt.
Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily
Abhishek Chatterjee;Yue Li;Yang Zhang;Tyler L Grove.
Nature Chemical Biology (2008)
Radical S-Adenosylmethionine Enzymes in Human Health and Disease
Bradley J. Landgraf;Erin L. McCarthy;Squire J. Booker.
Annual Review of Biochemistry (2016)
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