Squire Booker
Evan Pugh Professor of Chemistry; Professor of Biochemistry and Molecular Biology
-
104 Chemistry
University Park, PA 16802 - sjb14@psu.edu
- 814-865-8793
Research Summary
Elucidating the chemical mechanisms by which enzymes containing iron-sulfur clusters catalyze chemical reactions. Most ongoing projects deal with members of the Radical S-adenosylmethionine Superfamily, a diverse group of enzymes that employ radical chemistry to catalyze transformations involved in post-transcriptional and post-translational modifications, cofactor biosynthesis, secondary metabolite biosynthesis, and enzyme activation.
Huck Affiliations
Links
Publication Tags
S Adenosylmethionine Enzymes Proteins Iron Methylation Substrates Electrons Aldehydes Biosynthesis Formic Acid Oxygenases Oxidation Reduction Escherichia Coli Peptides Fatty Aldehyde Vitamin B 12 Aldehyde Decarbonylase Peroxides Acids X Ray Crystallography Nosiheptide Methyltransferases Carbon Monoxide Sulfur CatalysisMost Recent Papers
An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase
Olga A. Esakova, Alexey Silakov, Tyler L. Grove, Douglas M. Warui, Neela H. Yennawar, Squire J. Booker, 2019, Journal of the American Chemical Society on p. 14142-14151
Understanding the role of electron donors in the reaction catalyzed by Tsrm, a cobalamin-dependent radical S-adenosylmethionine methylase
Anthony J. Blaszczyk, Hayley L. Knox, Squire J. Booker, 2019, Journal of Biological Inorganic Chemistry on p. 831-839
Analysis of RNA Methylation by Phylogenetically Diverse Cfr Radical S-Adenosylmethionine Enzymes Reveals an Iron-Binding Accessory Domain in a Clostridial Enzyme
James D. Gumkowski, Ryan J. Martinie, Patrick S. Corrigan, Juan Pan, Matthew R. Bauerle, Mohamed Almarei, Squire J. Booker, Alexey Silakov, Carsten Krebs, Amie Kathleen Boal, 2019, Biochemistry on p. 3169-3184
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
Bo Wang, Joseph W. Lamattina, Savannah L. Marshall, Squire J. Booker, 2019, Journal of the American Chemical Society on p. 5788-5797
Stuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin Biosynthesis
Trey A. Ronnebaum, Jeffrey S. McFarlane, Thomas E. Prisinzano, Squire J. Booker, Audrey L. Lamb, 2019, Biochemistry on p. 665-678
The A-type domain in Escherichia coli NfuA is required for regenerating the auxiliary [4Fe– 4S] cluster in Escherichia coli lipoyl synthase
Erin L. McCarthy, Ananda N. Rankin, Zerick R. Dill, Squire J. Booker, 2019, Journal of Biological Chemistry on p. 1609-1617
Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis
Erin L. McCarthy, Squire J. Booker, 2018, Methods in Enzymology
Using Peptide Mimics to Study the Biosynthesis of the Side-Ring System of Nosiheptide
Bo Wang, Joseph W. LaMattina, Edward D. Badding, Lauren K. Gadsby, Tyler L. Grove, Squire J. Booker, 2018, Methods in Enzymology
Efficient methylation of C2 in L-tryptophan by the cobalamin-dependent radical S-adenosylmethionine methylase TsrM requires an unmodified N1 amine
Anthony J. Blaszczyk, Bo Wang, Alexey Silakov, Jackson V. Ho, Squire J. Booker, 2017, Journal of Biological Chemistry on p. 15456-15467
Transformations of the FeS Clusters of the Methylthiotransferases MiaB and RimO, Detected by Direct Electrochemistry
Stephanie J. Maiocco, Arthur J. Arcinas, Bradley J. Landgraf, Kyung Hoon Lee, Squire J. Booker, Sean J. Elliott, 2016, Biochemistry on p. 5531-5536
Most-Cited Papers
A radically different mechanism for S-adenosylmethionine-dependent methyltransferases
Tyler L. Grove, Jack S. Benner, Matthew I. Radle, Jessica H. Ahlum, Bradley J. Landgraf, Carsten Krebs, Squire J. Booker, 2011, Science on p. 604-607
Structural basis for methyl transfer by a radical SAM enzyme
Amie Kathleen Boal, Tyler L. Grove, Monica I. McLaughlin, Neela Yennawar, Squire J. Booker, Amy C. Rosenzweig, 2011, Science on p. 1089-1092
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase
Douglas M. Warui, Ning Li, Hanne Nørgaard, Carsten Krebs, J. Martin Bollinger, Squire J. Booker, 2011, Journal of the American Chemical Society on p. 3316-3319
Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase
Ning Li, Hanne Nørgaard, Douglas M. Warui, Squire J. Booker, Carsten Krebs, J. Martin Bollinger, 2011, Journal of the American Chemical Society on p. 6158-6161
Radical S-Adenosylmethionine Enzymes in Human Health and Disease
Bradley J. Landgraf, Erin L. McCarthy, Squire J. Booker, 2016, Annual Review of Biochemistry on p. 485-514
A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
Tyler L. Grove, Jessica H. Ahlum, Priya Sharma, Carsten Krebs, Squire J. Booker, 2010, Biochemistry on p. 3783-3785
RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins
Nicholas D. Lanz, Tyler L. Grove, Camelia Baleanu Gogonea, Kyung Hoon Lee, Carsten Krebs, Squire J. Booker, 2012, Methods in enzymology on p. 125-152
Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for s -adenosylmethionine
Tyler L. Grove, Matthew I. Radle, Carsten Krebs, Squire J. Booker, 2011, Journal of the American Chemical Society on p. 19586-19589
Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate
Maria E. Pandelia, Ning Li, Hanne Nørgaard, Douglas Warui, Lauren J. Rajakovich, Wei Chen Chang, Squire J. Booker, Carsten Krebs, Joseph M. Bollinger, Jr., 2013, Journal of the American Chemical Society on p. 15801-15812
X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry
Peter J. Goldman, Tyler L. Groèe, Squire J. Booker, Catherine L. Drennan, 2013, Proceedings of the National Academy of Sciences of the United States of America on p. 15949-15954