2012 Recipients

Eli Lilly Award in Biological Chemistry

Professor Christopher J. Chang, University of California, Berkeley.

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

Professor Christopher J. Chang is the recipient of the 2012 Eli Lilly Award in Biological Chemistry, in recognition of his contributions to discovery and understanding of new chemical signaling agents in biological systems. More specifically, Chang and his co-workers have developed molecular imaging probes that permit them to visualize the real-time production and/or trafficking of specific reactive oxygen species and metal ions in living cells and animals. These chemical tools have allowed the discovery and elucidation of new signal transduction pathways in a variety of models, including brain neurons, stem cells, adipocytes, cancer cells, and macrophages relevant to neurodegenerative and infectious diseases, cancer, diabetes, obesity, and regenerative medicine. For example, Dr. Chang has recently discovered that specific types of aquaporins, which are known to control the entry of water into cells and hence regulate osmotic pressure, can also function as channels for hydrogen peroxide, a molecule that is involved in redox signaling pathways. He will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.

Pfizer Award in Enzyme Chemistry

Professor Jin Zhang, Johns Hopkins University.

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

Professor Jin Zhang is the recipient of the 2012 Pfizer Award in Enzyme Chemistry, in recognition of her pioneering work in elucidating the spatiotemporal regulation of signaling molecules within the living cell. More specifically, she and her co-workers have developed novel genetically encoded fluorescent biosensors and applied them in living cells to track the activities of signaling enzymes such as protein kinases and phosphatases, which must be precisely regulated in both cellular space and time to perform their biological function. To date, these efforts have yielded an ever-expanding repertoire of fluorescent biosensors including reporters for PKA, PKC, Akt, c-jun N-terminal kinase, calcineurin, cAMP and phosphoinositides. Dr. Zhang’s laboratory has also devised new strategies to manipulate biochemical events inside living cells, which have served to unveil many of the molecular secrets underlying cell information processing, such as the identification of oscillatory kinase activities as a new mode of signal transmission. Her work is therefore establishing spatiotemporal regulation as a fundamental paradigm in cell signaling, with significant implications for (i) our understanding of both normal cell physiology and disease states, and (ii) enzyme function in living cells. She will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.

The Repligen Award in Chemistry of Biological Processes

Professor Carol Fierke, University of Michigan.

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

Professor Carol Fierke is the recipient of the 2012 Repligen Award in the Chemistry of Biological Processes, in recognition of her contributions to our broad understanding of how protein and nucleic acid catalysts achieve high efficiency with rigorous control of reaction specificity. In addition to her work on catalysis, Fierke and co-workers have made a number of significant contributions to our view of metal ion homeostasis in cells. 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. More specifically, 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, thereby permitting them to analyze cellular zinc homeostasis. She has also identified the biological metal cofactor and elucidated the catalytic mechanism of several other metalloenzymes, including protein farnesyltransferase, histone deacetylase and ribonuclease P. These studies have often led to unexpected conclusions that change the field. For example, she showed that the substrate for the ribozyme catalyst in ribonuclease P, which is only active as a protein/RNA complex, was actually bound by the protein subunit in contrast to previous hypotheses. Her work has also led to the novel proposal that cells may regulate enzyme activity by switching metals in the active site. More recent efforts to identify and quantify the in vivo substrates of enzymes that catalyze post-translational modifications have enhanced our understanding of the role of these modifications in biological pathways. Her ability to integrate ideas and methods from a variety of scientific disciplines to determine fundamental details about catalytic activity and cellular function is a hallmark of Professor Fierke’s work, which is important for efforts to develop enzyme inhibitors as therapeutic agents. She will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.

Gordon Hammes ACS Biochemistry Lectureship

Professor Angela Gronenborn, University of Pittsburgh.

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 Angela Gronenborn will present the Gordon Hammes ACS Biochemistry lecture at the Fall 2012 National Meeting of the American Chemical Society, in recognition of her pioneering achievements in the development of NMR methodologies for the determination of biomolecular structure, and in their subsequent application to proteins of particular biological interest. More specifically, she played a key role in employing constrained molecular dynamics and simulating annealing strategies to generate protein structures from NMR-derived distance restraints, and she and her group were leaders in using multi-dimensional, heteronuclear spectroscopic methods to extend NMR methods for the study of higher molecular weight molecules. Her invention of a novel PCR-based approach to prepare DNA that is uniformly isotopically labeled on a large scale has facilitated the detailed study of both the structure and dynamical properties of this class of biopolymer. Using the techniques that she pioneered, Dr. Gronenborn has been able to solve the structures of many cytokines and chemokines, which play critical roles in cell-cell signaling, and many proteins that are relevant to the biology of human immunodeficiency virus (HIV), including cyanovirin N, which inhibits HIV infection. She has also sought to elucidate the structure and dynamics of transiently formed complexes that are critical for cellular regulation and signaling but which are not amenable to study by X-ray crystallography. This work includes the mechanical processes by which the interaction of the SRY protein with its target DNA sequence induces a kink into the DNA. Her efforts to develop and harness the power of NMR for studying the three-dimensional structure of large proteins have opened new vistas for research upon the relationship between structure, dynamics and biological function.

The ACS Chemical Biology Lectureship

Professor Carolyn Bertozzi, University of California, Berkeley.

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

Professor Carolyn Bertozzi will present the 2012 ACS Chemical Biology lecture at the Spring 2012 National Meeting of the American Chemical Society, in recognition of her numerous contributions to chemical biology, which bridge the gap between molecular chemistry and biological function. As a leading innovator in the field, she developed reagents for “bioorthogonal chemistry”, most notably those for Staudinger ligation and copper-free “click” chemistry, which permit chemists to carry out synthetic chemistry transformations within the complex chemical milieu that is present in cellular environments. These tools were originally designed to image cancer-specific cell-surface sugars, but their utility extends to many problems in chemical biology. For example, the Staudinger ligation chemistry has permitted her to perform advanced imaging studies in simple animal models, such as zebrafish, opening up new possibilities for understanding the spatial and temporal events that take place during growth and differentiation. Moreover, her development of a “genetically-encoded aldehyde tag” is a simple and elegant solution to the problem of site-specifically modifying protein structures in the cell, which is currently being commercialized to yield new protein-based therapeutics. Her tools have also revolutionized both the study of complex carbohydrates that decorate the cell surface and mediate cell-cell interactions, and provided chemists with the ability to “tag” specific molecules on the cell surface. Finally, she and her co-workers are trying to elucidate the biological functions of sulfated sugars, with a particular focus on the sulfotransferase enzymes that are used to assemble these molecules. Importantly, Professor Bertozzi has discovered that the properties of these enzymes are highly dependent on their location in specific regions of the cell, and recent work upon sulfur metabolism during mycobacterial infections has allowed her to identify a promising new target for the development of therapeutics against tuberculosis.

Murray Goodman Memorial Prize

Professor Jeffrey Kelly, The Scripps Research Institute.

For contributions.

The 2012 Goodman Award, sponsored by Biopolymers is awarded to Jeffery Kelly. The symposium for this award will be held at the Fall ACS meeting in Philadelphia in August 2012