Recipients

Eli Lilly Award in Biological Chemistry

Professor Matthew D. Disney, Scripps, Florida.

For outstanding research in biological chemistry of unusual merit and independence of thought and originality.

Professor Matthew D. Disney is the recipient of the 2013 Eli Lilly Award in Biological Chemistry, in recognition of his contributions to the development of rational and potentially general methods to design small molecules that target and manipulate the cellular function of RNA. The development of small molecules that target RNA has been a long-standing challenge in chemical biology. This has been due to a fundamental lack of understanding of the RNA motifs that are good targets for small molecules and the types of small molecules that specifically recognize RNA motifs. Disney and co-workers developed a sensitive and high throughput approach, called two-dimensional combinatorial screening, to rapidly fill this information void by defining optimal small molecule-RNA motif partners. These partners are then mined against RNA sequence to design small molecules that specifically target RNAs that contribute to incurable diseases. Designed compounds recognize RNA targets with affinities and selectivities that far exceed that of natural proteins. Since RNA contributes to many diseases, these studies can have far-reaching implications in both the development of therapeutics or chemical probes to understand the cellular function of RNA. He will present a lecture as part of a symposium at the Fall 2013 ACS National Meeting.

Pfizer Award in Enzyme Chemistry

Professor Kate Carroll, Scripps, Florida.

For outstanding work in enzyme chemistry where the presence of enzyme action is unequivocally demonstrated.

Professor Kate Carroll is the recipient of the 2013 Pfizer Award in Enzyme Chemistry, in recognition of her contributions to discovery and understanding of cysteine oxidation events as biologically important post-translational protein modifications. More specifically, she and her co-workers have developed novel chemical probes that permit them to track and visualize specific cysteine ‘oxoforms’ within living cells. These chemical tools have allowed the discovery and elucidation of cysteine S-oxidation as a new paradigm in signal transduction and the regulation of protein function. For example, Dr. Carroll has recently discovered that hydrogen peroxide, a signaling molecule generated by membrane-bound NADPH oxidases, can oxidize a conserved cysteine residue in the active site of the epidermal growth factor receptor. This targeted modification stimulates the receptor’s intrinsic tyrosine kinase activity, which increases cell survival, proliferation, and growth. These findings, and others recently reported by her group, have important therapeutic implications for age-related illnesses, such as cancer, cardiovascular disease, inflammatory conditions, and neurodegenerative disorders. She will present a lecture as part of a symposium at the Fall 2013 ACS National Meeting.

The Repligen Award in Chemistry of Biological Processes

Professor David W. Christianson, University of Pennsylvania.

For outstanding contributions to the understanding of biological processes with particular emphasis on structure, function and mechanism.

Professor David W. Christianson is the recipient of the 2013 Repligen Award in the Chemistry of Biological Processes, in recognition of his contributions to our understanding of the structure and function of metal-requiring enzymes. He pioneered structural studies of the arginase family of enzymes, and his subsequent structural analyses of arginase-related deacetylases such as polyamine and histone deacetylases have illuminated the divergence of metal ion stoichiometry, specificity, and chemistry in the evolution of the arginase fold in all forms of life. These studies have had a translational component as well, with the validation of arginase as a drug target for cardiovascular disease and the development of boronic acid-based inhibitors as drug leads. Christianson has also made remarkable discoveries regarding the structure and function of terpenoid cyclases. Starting with just a handful of linear isoprenoid substrates, these enzymes catalyze the first committed steps of biosynthetic pathways leading to the formation of more than 60,000 different terpenoid natural products. Christianson’s studies have illuminated the evolution of modular enzyme architecture and active site templates that direct multi-step cyclization cascades. In essence, the vast chemodiversity of cyclic terpenoids is rooted in three cyclase modules that can be mixed and matched by nature or by design. Christianson will present a lecture as part of a symposium at the Fall 2013 ACS National Meeting.

Gordon Hammes ACS Biochemistry Lectureship

Professor Christopher T. Walsh, Harvard University.

For outstanding contributions in scientific research at the interface of chemistry and biology, particularly in the realm of biochemistry, biological chemistry and molecular biology.

Professor Christopher T Walsh will present the 2013 Gordon Hammes ACS Biochemistry Lecture at the Fall 2013 National Meeting of the American Chemical Society in recognition of his research achievements in deciphering novel chemical transformations and enzymatic machinery in the biosynthesis of biologically active natural products. Walsh and coworkers have described enzymes that make and break cyclopropane rings, carry out Baeyer-Villiger insertions, convert peptide bonds to heterocycles, cleave organomercury carbon-Hg bonds and reduce Hg++ to Hgo ,nickel enzymes in methanogenic bacteria that carry out enzymatic carbonylation and hydrogenation reactions, and a novel class of mononuclear nonheme iron halogenases. Walsh and colleagues have characterized enzymatic assembly lines and post-assembly tailoring enzymes for biosynthesis of polypeptide, polyketide and hybrid polyketide/polypeptide antibiotic and antitumor agents. A major area of Walsh’s research activity has been in mechanism of action of and resistance to antibiotics from fosfomycin to vancomycin and most recently the posttranslational cascades that generate the thiazolyl peptide class of antibiotics.

The ACS Chemical Biology Lectureship

Professor Wilfred A. van der Donk, University of Illinois, Urbana-Champaign

For contributions that have had a major impact on scientific research in the area of Chemical Biology.
 

Professor Wilfred van der Donk will present the 2013 ACS Chemical Biology Lecture at the Spring 2013 ACS National Meeting in recognition of his contributions to understanding enzyme reaction mechanisms. His laboratory determined the structures of radical intermediates generated by prostaglandin H synthase by using synthetic isotopically labeled arachidonic acid substrates, and studied the mechanism of phosphite dehydrogenase, an enzyme that catalyzes a nucleophilic substitution reaction with a hydride leaving group. He and his coworkers also provided insights into vitamin B12-catalyzed dechlorination of the priority pollutants perchloroethylene and trichloroethylene. More recently, his group studied the biosynthesis of natural products, including lantibiotics, phosphonates, and S-linked glycopeptides. The topics of these investigations include the cyclase that generates five thioether rings in nisin, a non-heme iron dependent enzyme that cleaves an unactivated carbon-carbon bond during the biosynthesis of the herbicide phosphinothricin, and a related enzyme that generates methylphosphonate, the likely substrate for methane production in the oceans. Van der Donk and colleagues have used their understanding of natural product biosynthesis for genome mining efforts that to date have uncovered more than 30 new natural products.

Murray Goodman Memorial Prize

To Be Announced

For contributions.