Eli Lilly Award in Biological Chemistry

Professor Elizabeth M. Nolan, Massachusetts Institute of Technology

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


Professor Elizabeth M. Nolan is the recipient of the 2016 Eli Lily Award in Biological Chemistry in recognition of her contributions to metal homeostasis and human innate immunity. Her research program is motivated by the global public health problems of infectious disease and antibiotic resistance, and affords paradigms for the discovery and elucidation of new bioinorganic chemistry, advancing fundamental understanding of human innate immunity and microbial pathogenesis, and providing new molecules with potential therapeutic application. Her recent initiatives focus on deciphering the biochemical and biophysical properties of biomolecules employed by the human host and colonizing microbe at mucosal surfaces and sites of infection. Metal ions are essential nutrients for all organisms, and one strategy the human innate immune system employs to prevent microbial colonization involves the deployment of metal-chelating proteins that sequester nutrient metals (e.g. manganese, iron, zinc) from invading microbes in the extracellular space. Her laboratory has illuminated the bioinorganic chemistry of human calprotectin, an abundant neutrophil protein that sequesters first-row transition metals at sites of infection. Her group recently discovered that human calprotectin sequesters ferrous iron at an unusual hexahistidine site, which expands the biological coordination chemistry of non-heme iron. Her laboratory also pursues biochemical and biophysical studies of two cysteine-rich defensin peptides, human α-defensin 5 and 6, that are abundant in the human small intestine and contribute to intestinal homeostasis. Towards the discovery and development of new strategies to treat infectious disease, her group studies the chemistry and biology of siderophores, small-molecule iron chelators that are biosynthesized by bacteria seeking to replicate in iron-limited environments. Her research focuses on employing native siderophore scaffolds in targeted antibiotic delivery, and on identifying new strategies to block siderophore-mediated iron acquisition by bacterial pathogens.

Pfizer Award in Enzyme Chemistry

Professor Michelle C. Chang, University of California, Berkeley

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


Professor Michelle C. Chang is the recipient of the 2016 Pfizer Award in Enzyme Chemistry in recognition of her contributions to the understanding of enzymatic incorporation of fluorine into natural products.  Her research group works at the interface of enzymology and synthetic biology, with a focus on understanding and engineering enzymes and metabolic networks involved in the production of pharmaceuticals, materials, and commodity chemicals. In particular, her laboratory has focused on developing synthetic biology approaches to introduction of fluorine into small molecule targets, which has become a key strategy for drug design and discovery. Although fluorine has emerged as a common design element among man-made compounds, only a handful of biogenic compounds containing fluorine (<20) from the fluoroacetate pathway of Streptomyces cattleya have been identified to date. Her research group has studied the mechanism of fluorine selectivity in a fluoroacetyl-CoA thioesterase from S. cattleya and showed that it is mediated by catalysis rather than substrate recognition. They have further shown that thioester hydrolysis proceeds by an unusual Cα-deprotonation mechanism through a putative ketene intermediate. This work has enabled the engineering of systems for the enzymatic introduction of the fluoroacetate monomer into polyketide products.

The Repligen Award in Chemistry of Biological Processes

Professor Tadhg Begley, Texas A&M University

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


Professor Tadhg P. Begley is the recipient of the 2016 Repligen Award in the Chemistry of Biological Processes in recognition of his contributions to mechanistic enzymology of cofactor biosynthesis. Focusing on complex cofactor assembly reactions, he has uncovered a remarkable amount of new biochemistry demonstrating nature’s versatility in assembling these key metabolites. His most significant contribution involves the biosynthesis of thiamin pyrophosphate. He elucidated the mechanistic chemistry of thiazole and pyrimidine formation in both bacteria and yeast. Highlights of this work include the discovery that the bacterial thiamin pyrimidine is formed by a complex radical SAM-mediated rearrangement as well as the discovery of a small sulfide carrier protein involved in the thiazole biosynthesis. Similar sulfide carrier proteins have now been found in the biosynthesis of other key metabolites. The discovery that two suicidal enzymes mediate the thiazole and pyrimidine assembly in yeast was unexpected. In these enzymes, part of the reaction product is derived from the enzyme. The biological functions of the resulting posttranslational modifications have yet to be elucidated. Begley has also characterized the thiaminase-mediated thiamin degradation as well as the biosynthesis and mode of action of bacimethrin – the only known anti-thiamin natural product. The thiamin biosynthesis project benefitted greatly from a structural biology collaboration with Steve Ealick at Cornell that resulted in structures of all of the thiamin biosynthetic enzymes. The Begley group has also made important contributions to the biosynthesis of NAD, molybdopterin, menaquinone, pyridoxal phosphate, vitamin B12, coenzyme A and the deazaflavin F420. Current areas of research include the elucidation of the mechanism of complex radical rearrangements involved in cofactor biosynthesis, cofactor catabolism and prospecting for new catalytic motifs in flavo-enzymology.

Gordon Hammes ACS Biochemistry Lectureship

Professor Carol A. Fierke, University of Michigan

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 Carol A. Fierke is the recipient of the 2016 Gordon Hammes ACS Biochemistry Lectureship in recognition of her contributions toward understanding the function of enzymes.  Her laboratory has combined an array of chemical, biological and biophysical approaches to identify the mechanistic and structural constraints that determine the high catalytic efficiency and rigorous substrate specificity of protein and nucleic acid catalysts. She is recognized as an international leader in devising elegant experimental approaches for probing the structure, function and biological relevance of metals as cofactors in catalysis.  She and her co-workers carried out a groundbreaking analysis of the determinants of metal affinity and specificity for carbonic anhydrase, the prototypical zinc enzyme, and then used this information to develop biosensors to make the first real-time measurement of the cellular concentration of readily exchangeable zinc ions to analyze cellular zinc homeostasis.  Additionally, her work led to a detailed understanding of the catalytic mechanism and metal selectivity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase and histone deacetylase (HDAC) as well as demonstrating the feasibility of Zn/Fe metal switching in cells.   Her laboratory has investigated the substrate selectivity of enzymes that post-translational modifications, leading to a better understanding of their biological function.  Measurement of the reactivity of protein farnesyltransferase with peptide substrates taken from the human proteome demonstrated that hundreds of proteins are farnesylated in cells. Studies with HDAC8 have led to an understanding of the structural determinants of peptide recognition and the identification of in vivo substrates.   Finally, the Fierke lab elucidated the catalytic mechanism, substrate selectivity and structural transitions of both an RNA—dependent and a protein-dependent ribonuclease P that catalyze maturation of precursor-tRNA, demonstrating that both enzymes use comparable two-metal ion catalytic mechanisms.  Fierke’s work significantly enhanced our understanding of the cellular function of all of these enzymes and the potential for therapeutic interventions by enzyme-specific inhibitors.

The ACS Chemical Biology Lectureship

Professor Peter G. Schultz, The Scripps Research Institute

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


Professor Peter G. Schultz is the recipient of the 2016 ACS Chemical Biology Lectureship. Schultz’s research uses both chemical and biological tools to synthesize molecules with novel functions. By developing technologies to make and characterize molecules and materials hundreds to million at a time, his work has dramatically impacted our ability to make create molecules with novel biological and physical properties-ranging from medicines to materials. He has pioneered the development of new drugs that affect endogenous stem cells for neurodegenerative diseases and diseases of aging, and has led efforts that have resulted in breakthrough therapies for the treatment of multiple sclerosis, lung and blood cancers, and malaria. At the same time his work has changed the way both academic and industrial scientists discover new catalysts, polymers and energy storage materials. Most recently his laboratory has successfully created new “synthetic” organisms in which the evolutionary constraints of the twenty-amino acid genetic code are lifted. This advance is allowing scientists to create new biomolecules and even whole organisms with properties that are not possible using Mother Nature’s restricted set of protein building blocks.

The Biopolymers Murray Goodman Memorial Prize

Professor Jennifer Doudna, University of California, Berkeley

For outstanding accomplishments in one or more of the areas of biochemistry, biophysical chemistry, biophysics, and/or chemical biology.


Professor Jennifer A. Doudna is the recipient of the 2016 Biopolymers Murray Goodman Memorial Prize. Doudna’s research focuses on determining how non-coding RNAs function in living systems. Following her pioneering work on the structures and catalytic mechanisms of ribozymes, Dr. Doudna made exceptional advances in understanding how small RNAs are produced and used to control gene expression in mammals and bacteria. This line of research led to the breakthrough discovery of an RNA-programmed DNA endonuclease, Cas9, which functions as part of a CRISPR-based acquired immunity system in bacteria. By determining the molecular mechanism by which Cas9 uses RNA to recognize and cleave double-stranded DNA at specific sites, Doudna and collaborator Emmanuelle Charpentier showed how the system could be readily adapted for use in human and other cells and organisms. This transformative technology has influenced fundamental and clinical biology by enabling genetic experiments that were previously difficult or impossible to conduct. As Doudna’s research revealed, the CRISPR-Cas9 enzyme functions by using a 20-nucleotide RNA sequence within a dual-guide RNA structure to base pair with a complementary target sequence within doubled-stranded DNA. By showing how the dual-guide RNA could be redesigned as a single-guide RNA with the necessary structure to bind Cas9 and to direct site-specific Cas9-mediated DNA cleavage, Doudna and Charpentier’s findings almost immediately became a transformative tool for molecular biologists. The CRISPR-Cas9 system has been used for site-specific genome editing in human somatic and pluripotent stem cells, mice, rats, plants, fruit flies, nematodes and fungi. This versatile system is useful in organisms and cell lines, and also in various ex vivo experiments where excision of specific segments of chromosomes is desirable. The CRISPR-Cas9 technology is likely to create new therapeutic strategies as well as impacting the fields of plant and synthetic biology.