Squire Booker

Evan Pugh Professor of Chemistry; Professor of Biochemistry and Molecular Biology

Squire Booker

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 Catalysis

Most 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