Lester Reed: A "complex" man who loved science.

Lester J. Reed, a pioneer in the field of biochemistry, died peacefully in Austin, Texas on January 14, 2015 at the age of 90. Lester Reed was born in New Orleans on January 3, 1925. He showed an early interest in chemistry, having his own laboratory in a shed under his boyhood home. He received his Bachelors of Science from Tulane in 1943, where he worked with William Shive, and earned his doctorate from the University of Illinois in 1946, where he worked with Reynold Fuson. Lester was 21 when he earned his doctorate. He then moved to Cornell University Medical School for a two-year postdoctorate in the laboratory of Vincent du Vigneaud. Two momentous events occurred during this short period: Lester was introduced to the field of biochemistry, and he met and married the love of his life, Janet Gruschow. In 1948, at age 23, Lester was recruited to the Chemistry Department at the University of Texas at Austin by Shive, who had moved there from Tulane. He joined a team led by Roger Williams studying vitamins. Lester isolated and identified the “acetate-replacing factor,” first observed by Esmond Snell, as lipoic acid. Later, working in collaboration with Eli Lilly and Co., they were able to purify about 30 mg of lipoic acid from over 10 tons of liver tissue! Wanting to know more about the functional role of this simple but unique organic compound, Lester discovered that lipoic acid was bound to a protein involved in the CoAand NAD-linked oxidative decarboxylation of pyruvate and α-ketoglutarate. Thus began a trail of five decades of research to study the mechanism of oxidative decarboxylation of α-keto acids. Lester’s laboratory determined that the protein involved was part of a large complex. He and his colleagues were able to isolate and characterize the component enzymes (E1, E2, and E3), and then reassemble the large, functional multienzyme complexes responsible for these reactions. The lipoic acid was covalently attached to the E2 component that had both catalytic and structural roles, binding the other components. Lester’s laboratory used electron microscopy to discover that there were two different architectural forms of these large complexes (the cube with 24 E2 subunits and the pentagonal dodecahedron with 60 E2 subunits), and went on to propose a novel “swinging-arm” active-site coupling mechanism to explain how multiple copies of these three enzymes were able to efficiently catalyze successive reactions using five vitamin-related cofactors. The next major discovery was that two additional components (kinase and phosphatase) were involved in the regulation of the activity of these complexes via phosphorylation/ dephosphorylation, which today is recognized as a common regulatory control mechanism. Reflective of Lester’s remarkable scientific career, he received the Eli Lilly Award in 1958 (age 33), was elected to the National Academy of Sciences in 1973 (age 48), was elected a Fellow of the American Academy of Arts and Sciences in 1981, won the Merck Award in 1994, and served as Director of the Biochemical Institute at The University of Texas at Austin from 1963 to 1996. During his 51 years on the faculty at The University of Texas, the trio of Lester Reed, Roger Williams, and William Shive, along with Esmond Snell, Robert Eakin, and Karl Folkers, were responsible for the isolation, naming, and characterization of more vitamins than at any other place in the world. To many of his scientific colleagues, Lester was a quiet, even shy person who often stayed out of the spotlight, but he had that gleam in his eyes that made you know that there was a lot of intensity in this man. Although Lester had a very competitive spirit when it came to his science, one had to be impressed by the high principles that characterized his science. Lester was always very careful and precise in his work. This was true in his writing, as evidenced in over 200 publications, and in his speech: he expressed his thoughts clearly and concisely, and he always told you just what he thought. Lester had a very dry but amazing sense of humor. Often he would crack a joke, and then break into that familiar, broad smile. Outside the laboratory, Lester enjoyed boating and fishing, and he never missed the annual weekend outing of the central Texas Society of Applied Piscatology. Lester and Janet were a true team. They settled into Austin in 1948 and put down deep roots in the community. By 1960 they had welcomed their four children: Pam, Sharon, Richard, and Robert. Photos of a relaxed, young Lester playing with his kids, or sipping a drink while enjoying their pool, reveal a loving husband, father, and later in life, a very proud grandparent. Lester Reed was a member of Phi Beta Kappa, Sigma Xi, the American Chemical Society, the American Society for Biochemistry and Molecular Biology, The Protein Society, and the American Association for the Advancement of Science. He served on many advisory councils and editorial boards, and was the recipient of several national honors. In 1997, his wife Janet Reed created the Lester J. Reed Professorship in Biochemistry at the University of Texas at Austin to honor Lester and his love of science. He will be missed by his colleagues, friends, family, and many former students and postdoctorates around the world. Those of us that were lucky enough to know him were richly blessed.