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= Squire Booker =

Dr. Squire Booker is an African American biochemistry researcher at Penn State University. He researches biochemistry, enzymology, protein chemistry, natural product biosynthesis, and mechanisms of radical dependent enzymes. He is an associate editor for the American Chemical Society Biochemistry Journal. He is a Howard Hughes Medical Institute Investigator. He is an Eberly Distinguished Chair in Science at Penn State University.

Early Years
Dr. Booker grew up in the segregated community of Beaumont, Texas. He was raised by his grandmother with the help of three uncles. He grew up not hearing much praise about African Americans in science.

Education
Dr. Booker received his Bachelors of Arts in Chemistry at Austin College in 1987, where he was a Minnie Stevens Piper Scholar. He received his Ph.D. in Biochemistry from Massachusetts Institute of Technology in 1994. He researched as a postdoctorate at Universite Rene Decartes in Paris, France. He had a Postdoctoral Fellowship at the Institute for Enzyme Research at the University of Wisconsin. He became a professor at Penn State University in 1999.

Research
Dr. Booker is a professor of biology, biochemistry, and molecular biology at Penn State University. He is interested in how enzymes change their catalytic abilities due to metal ions or metal clusters. His research focuses on enzymes containing iron-sulfur clusters which catalyze chemical reactions. He focuses on the Radical S-adenosylamethionine Superfamily (SAM) which is a group of enzymes that encounters radical chemistry in post-transcriptional and post-translational modifications of DNA.

He also researches many bacteria including Staphlococcus aureus which often lives in noses and on skins of humans. Staphlococcus aureus is problematic because it can mutate into MRSA (methicillin resistant Staphylococcus aureus) which is highly resistant bacteria. There is a protein called Cfr protein in Staphlococcus aureus that binds to the ribosome which is where translation occurs. Many antibiotics bind to ribosomes which cause bacteria to die. However, when Cfr is expressed, it binds to the ribosome and allows the bacteria to stay alive which is known as methylation This research has led Dr. Booker to discover that Staphlococcus aureus expresses a protein, Cfr, which makes it resistant to many antibiotics. He developed mechanism of this methylation. Dr. Booker's lab also researches aspects of the bacterium, Escherichia coli. He determined the three-dimensional structure of the RImN protein from the bacteria. RImN is one of two proteins which makes chemical modification to different RNA molecules. Understanding this structure will help with other research of antibiotic resistance. As a result of his research, he is synthesizing new compounds to stop the bacteria's defenses which would make antibiotics more effective. The goal of his research to design compounds which can prevent infections due to drug-resistant bacteria.

Activism
Dr. Booker is active in promoting diversity in Science, Technology, Engineering, and Mathematics (STEM). He was a chair on the Minority Affairs Committee of the American Association of Biochemistry and Molecular Biology. In 2010, he helped organize a workshop which discussed the different obstacles and challenges that minorities in biochemistry and molecular biology encounter when building externally funded research programs.

Dr. Booker was the guest speaker at Massachusetts Institute of Technology's 2019 Investiture of Doctoral Hoods and Degree Conferral Ceremony. He was chosen to due his impressive contributions to the scientific community and his activism towards inclusion of all in STEM. In his speech, he emphasized an opportunity for all in science. He encouraged the graduates to take responsibility and give back to society. It does not matter what one's background is in, people in STEM need to be willing to accept and stand up for each other.

Honors and Awards
Dr. Booker has received numerous honor and awards, but here is just a few of the most notable ones.


 * 2019 Associate Editor for the American Chemical Society Biochemistry Journal
 * 2018 Evan Pugh Professor at Penn State University
 * 2017 Eberly Distinguished Chair in Science at Penn State University
 * 2017 Elected to the American Academy of Arts and Sciences
 * 2017 Lloyd N. Ferguson Distinguished Lecturer at Cal State, Los Angeles
 * 2016 Penn State Faculty Scholar Medal
 * 2016 Scott Lectureship in Chemistry and Biochemistry at the University of Florida
 * 2016 Co-organizer of the ASBMB Annual Meeting
 * 2015 Selected as a Howard Hughes Medical Investigator
 * 2015 Everson Lectureship in Biochemistry at the University of Wisconsin, Madison
 * 2014 Fellow of the American Association for the Advancement of Science
 * 2013 TY Shen Lectureship in Biological Chemistry at MIT
 * 2011 American Chemical Society Arthur C. Cope Scholar Award
 * 2006 Co-Chair, GRC on Enzyme Coenzymes and Metabolic Pathways
 * 2004 Presidential Early Career Award in Science and Engineering
 * 2002-2007 NSF Faculty Early Career Award
 * 1996-1999 NIH Postdoctoral Fellow at the Institute for Enzyme Research at the University of Wisconsin
 * 1994-1995 NSF-NATO Postdoctoral Fellow

Publications
Dr. Booker has published over 100 scientific publications in journals such as the Journal of the American Chemical Society and Proceedings of the National Academy of Sciences. Dr. Booker has published numerous scientific articles, but here is just a few of the most notable ones.


 * Mccarthy, E. L.; Rankin, A. N.; Dill, Z. R.; Booker, S. J. The A-Type Domain in Escherichia Coli NfuA Is Required for Regenerating the Auxiliary [4Fe–4S] Cluster in Escherichia Coli Lipoyl Synthase. Journal of Biological Chemistry 2018, 294 (5), 1609–1617.
 * Lanz, N. D.; Blaszczyk, A. J.; Mccarthy, E. L.; Wang, B.; Wang, R. X.; Jones, B. S.; Booker, S. J. Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia Coli. Biochemistry 2018, 57 (9), 1475–1490.
 * Mccarthy, E. L.; Booker, S. J. Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in Escherichia Coli Lipoyl Synthase During Catalysis. Methods in Enzymology Radical SAM Enzymes 2018, 217–239.
 * Blaszczyk, A. J.; Silakov, A.; Zhang, B.; Maiocco, S. J.; Lanz, N. D.; Kelly, W. L.; Elliott, S. J.; Krebs, C.; Booker, S. J. 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 2016, 138 (10), 3416–3426.
 * Mclaughlin, M. I.; Lanz, N. D.; Goldman, P. J.; Lee, K.-H.; Booker, S. J.; Drennan, C. L. Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase. Proceedings of the National Academy of Sciences 2016, 113 (34), 9446–9450.
 * Bauerle, M. R.; Schwalm, E. L.; Booker, S. J. Mechanistic Diversity of RadicalS-Adenosylmethionine (SAM)-Dependent Methylation. Journal of Biological Chemistry 2014, 290 (7), 3995–4002.
 * Rajakovich, L. J.; Nørgaard, H.; Warui, D. M.; Chang, W.-C.; Li, N.; Booker, S. J.; Krebs, C.; Bollinger, J. M.; Pandelia, M.-E. 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 2015, 137 (36), 11695–11709.
 * Grove, T. L.; Livada, J.; Schwalm, E. L.; Green, M. T.; Booker, S. J.; Silakov, A. A Substrate Radical Intermediate in Catalysis by the Antibiotic Resistance Protein Cfr. Nature Chemical Biology 2013, 9 (7), 422–427.
 * Grove, T. L.; Benner, J. S.; Radle, M. I.; Ahlum, J. H.; Landgraf, B. J.; Krebs, C.; Booker, S. J. A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases. Science 2011, 332 (6029), 604–607.
 * Boal, A. K.; Grove, T. L.; Mclaughlin, M. I.; Yennawar, N. H.; Booker, S. J.; Rosenzweig, A. C. Structural Basis for Methyl Transfer by a Radical SAM Enzyme. Science 2011, 332 (6033), 1089–1092.
 * Matthews, M. L.; Neumann, C. S.; Miles, L. A.; Grove, T. L.; Booker, S. J.; Krebs, C.; Walsh, C. T.; Bollinger, J. M. Substrate Positioning Controls the Partition between Halogenation and Hydroxylation in the Aliphatic Halogenase, SyrB2. Proceedings of the National Academy of Sciences 2009, 106 (42), 17723–17728.
 * Grove, T. L.; Lee, K.-H.; Clair, J. S.; Krebs, C.; Booker, S. J. In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters. Biochemistry 2008, 47 (28), 7523–7538.
 * Chatterjee, A.; Li, Y.; Zhang, Y.; Grove, T. L.; Lee, M.; Krebs, C.; Booker, S. J.; Begley, T. P.; Ealick, S. E. Reconstitution of ThiC in Thiamine Pyrimidine Biosynthesis Expands the Radical SAM Superfamily. Nature Chemical Biology 2008, 4 (12), 758–765.
 * Booker, S. J.; Cicchillo, R. M.; Grove, T. L. Self-Sacrifice in Radical S-Adenosylmethionine Proteins. Current Opinion in Chemical Biology 2007, 11 (5), 543–552.
 * Cicchillo, R. M.; Iwig, D. F.; Jones, A. D.; Nesbitt, N. M.; Baleanu-Gogonea, C.; Souder, M. G.; Tu, L.; Booker, S. J. Lipoyl Synthase Requires Two Equivalents OfS-Adenosyl-l-Methionine To Synthesize One Equivalent of Lipoic Acid. Biochemistry 2004, 43 (21), 6378–6386.
 * Cicchillo, R. M.; Lee, K.-H.; Baleanu-Gogonea, C.; Nesbitt, N. M.; Krebs, C.; Booker, S. J. Escherichia Coli Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide. Biochemistry 2004, 43 (37), 11770–11781.
 * Lieder, K. W.; Booker, S.; Ruzicka, F. J.; Beinert, H.; Reed, G. H.; Frey, P. A. S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic Resonance. Biochemistry 1998, 37 (8), 2578–2585.
 * 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 1994, 33 (42), 12676–12685.
 * Booker, S.; Stubbe, J. Cloning, Sequencing, and Expression of the Adenosylcobalamin-Dependent Ribonucleotide Reductase from Lactobacillus Leichmannii. Proceedings of the National Academy of Sciences 1993, 90 (18), 8352–8356