Friday, May 19, 2017 at Meridian Banquets
Starts at 7:00 PM · Ends on May 19, 2017 at 10:30 PM, EST (America/New_York)
106th Willard Gibbs Award Address:
Prof. Judith Klinman
- University of California, Berkeley -
Dept. of Chemistry
"C-H Activation, Quantum Tunneling, and New Ways of Looking at Enzyme Catalysis"
Our ability to understand and design potent catalysts lies squarely at the interface of biology and chemistry. In particular, the enormous rate accelerations of enzyme catalyzed reactions make them ideal subjects for advancing this topic. Yet, despite over half a century of inquiry, de novo design has failed to produce new enzyme catalysts that approximate the properties seen in Nature. This talk will focus on emergent properties that necessitate the incorporation of QM tunneling and protein motions as a central paradigm in enzyme function.
The Chicago Section has been awarding the Gibbs Medal annually since 1911, and it is one of the most prestigious prizes in chemistry. Many Gibbs awardees have proceeded to win the Nobel Prize and/or Priestley Medal, including Svante Arrhenius, Marie Curie, Linus Pauling, Carl Cori, and Rudy Marcus. We are pleased to add Prof. Klinman as the 106th member of this august company. The award ceremony attracts many of the top minds in chemistry and leaders of the American Chemical Society. More details about the history of the Gibbs Award are documented here: http://chicagoacs.org/Willard_Gibbs_Award
For ground breaking discoveries in enzyme catalysis which:
- Pioneered the application of kinetic isotope effects to the study of enzyme catalysis and mechanism.
- Demonstrated how proteins containing TPQ generate their own cofactors performing two different catalytic roles of biogenesis and catalysis.
- Launched the field of protein derived cofactor that mediates enzyme activity.
- Demonstrated anomalies in kinetic studies that led to the discovery that protein structures have evolved to catalyze effective quantum mechanical tunneling.
- 6:00 - 7:00 Registration and reception with hors d'oeuvres, and 2 complimentary drinks
- 7:00 - 8:30 Dinner
- 8:30 - 8:45 ACS Award Ceremony
- A History of the Willard Gibbs Award by Fran Kravitz, Chicago Section Chair
- Introduction of Professor Klinman by Brian Hoffman, Northwestern University
- Presentation of the Willard Gibbs Medal by Peter Dorhout, President-Elect of the American Chemical Society
- 8:45 - 9:30 Lecture by Prof. Klinman
- Soup: Cream of tomato basil bisque with bleu cheese
- Meridian Salad
- Choice of entree:
- BEEF: Roast top sirloin with rosemary merlot sauce
- SALMON: Fresh broiled Norwegian salmon with dill sauce
- VEGETARIAN: Portabello mushroom with zucchini
- Dessert: Hot fudge brownie a la mode
Dinner reservations are required and should be received by
Dinner Registration Deadline: 12:00 Noon on Tuesday, May 16
Lecture-only Registration Deadline: 12:00 Noon on Thursday, May 18
PLEASE HONOR YOUR RESERVATIONS. The Section must pay for all dinner orders. No-shows will be billed. Please contact the Section Office via phone (847-391-9091) or email (firstname.lastname@example.org) if you have any questions.
Dr. Klinman received her A.B. and Ph. D. from the University of Pennsylvania in l962 and l966 and then carried out postdoctoral research with Dr. David Samuel at the Weizmann Institute of Science, Israel, and Dr. Irwin Rose at the Institute for Cancer Research, Philadelphia. She was an independent researcher at the Institute for Cancer Research for several years, before moving to the University of California at Berkeley in l978, where she is now a Professor of the Graduate School in the Department of Chemistry, the Department of Molecular and Cell Biology, and the California Institute for Quantitative Biosciences (QB3).
Dr. Klinman has been focused on understanding the fundamental properties that underlie enzyme catalysis. Early in her career, she developed the application of kinetic isotope effects to the study of enzyme catalysis. In l990, she demonstrated the presence of the neurotoxin, 6-hydroxydopa quinone (referred to as TPQ), at the active site of a copper-containing amine oxidase from bovine plasma, overcoming years of incorrect speculation regarding the nature of the active site structure and opening up the field of protein-derived quino-cofactors. Subsequent work from her group showed that the extracellular protein lysyl oxidase, responsible for collagen and elastin cross-linking, contains a lysine cross-linked variant of TPQ, while mechanistic probes advanced knowledge of cofactor biogenesis and catalysis in the copper amine oxidases. Most recent work is focused on unraveling the enigmatic pathway for production of the free-standing bacterial cofactor/vitamin, pyrroloquinoline quinone.
Since the l990s, Klinman’s kinetic studies of enzyme reactions have demonstrated anomalies that demonstrate quantum mechanical hydrogen tunneling in enzyme-catalyzed hydrogen activation reactions. These findings indicate that proteins influence rate by modulating barrier width, not simply barrier height. Because the transfer of hydrogen as a wave requires restructuring of the heavy atom environment, her tunneling studies also provide a direct link between motions within a protein and the bond making/bond breaking processes that they catalyze. Many of the redox enzymes that have been pursued in the Klinman laboratory use molecular oxygen as substrate. She has developed a set of experimental probes for determining the mechanism of oxygen activation. These probes are able to shed light on how proteins can reductively activate O2 to free radical intermediates, while avoiding oxidative damage to themselves. Her most recent investigations are directed at expanding the principles uncovered from hydrogen transfer processes to other classes of enzyme reaction that include the large class of methyltransferases as well as the TIM barrel superfamily.
DIRECTIONS and PARKING:
1701 Algonquin Rd
Rolling Meadows, IL 60008
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$0.00 Individual Donation
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