Daniel Koshland dies

Daniel Koshland, who proposed a fundamental theory of how enzymes catalyze reactions and served as editor-in-chief of Science between 1985 and 1995, died Monday after suffering a stroke. He was 87.His research in biochemistry earned him multiple awards, including the Lasker Award and the National Medal of Science. During his tenure at Science, the journal's impact factor went up from 10.9 to 21.9.

Before Koshland, Science was known as a "sleepy journal," said Joseph Goldstein, a friend of Koshland's and a Nobel Laureate at the University of Texas Southwestern Medical Center at Dallas who said he has followed Koshland's work for 30 years. According to Richard Gallagher, editor and publisher of The Scientist, who was a senior editor of immunology and infectious diseases at Science from 1992 to 1999, the standards that Koshland set for selecting papers helped raise the journal's prominence.Koshland established a weekly "space meeting" in which editors selected the best submissions for publication. "He was always pretty tough on immunology," Gallagher said. "I used to study for it, I used to be nervous when I was ready to do my pitch."He also amended the peer-review process, establishing a "triage" stage of peer review, now a standard approach used to help pick exceptional papers from hundreds of submissions. Koshland recruited John Brauman, a researcher at Stanford University, to help increase coverage of the physical sciences. "He really pushed that direction," Brauman, currently the chair of the senior advisory board at Science, told The Scientist. "He put a lot of breadth into the biological sciences," he said, adding that Koshland had an eye for top-quality papers. "The journal was always important, but it went up a level after he got there.""He really turned it into an iconic journal that represented the real cutting edge forefront of science generally spread across the whole spectrum of scientific activity," Brauman said. Koshland's research in biochemistry focused on enzymology, bacterial sensing and bioenergy. In the late 1950s, he proposed a theory, called "induced fit," that explained how enzymes catalyze reactions in the body. Previously, researchers had thought an enzyme and substrate fit together rigidly like a lock fits in a key, said Goldstein. Koshland argued that the substrate instead stretches and rearranges the enzyme pocket, the way a hand fits in a glove. "That was a totally novel concept," Goldstein said. "That's the way proteins are viewed today." The study describing his theory was published in the Proceedings of the National Academy of Sciences in 1958 and has been cited almost 700 times.Koshland shifted his research in the 1970s to focus on how bacteria respond to their environments, a process called chemotaxis. He showed that bacteria have a basic memory that allows them to compare the past and present of their biochemical environments. His work on how receptors transduce chemical information has been used to explain the mechanisms underlying vision, hearing and smell. Andrew Mesecar, a former postdoctoral researcher who worked with Koshland from 1994 to 1998, said he and Koshland came up with another theory, called "orbital steering," that explained how small structural changes in a metabolic enzyme significantly changed the enzyme's catalytic power. They published the findings, cited over 100 times, in Science in 1997. Koshland understood experimental data broadly and would propose models that explained them, Mesecar, now a faculty member at University of Illinois in Chicago, told The Scientist. "And these models have been around for decades, and they are in textbooks. I just felt so privileged that I was accepted into his lab, to work with someone with so much scientific history," he said. More recently, Koshland switched the focus of his lab from the study of signal transduction to the field of bioenergy. The group began using photosynthesis in cyanobacteria to create methane, a possible source for alternative energy. In this process, cyanobacteria create acetic acid, which are fed to methanogens (bacteria-like, single celled organisms) to convert acetic acid to methane. Studying methanogens "was a gutsy call on Dan's part," because so few labs studied them, said Martin Lee, a postdoctoral researcher who joined Koshland's lab two months ago. "That's what we were only starting to do." Robert Tjian, professor of molecular and cell biology at UC Berkeley, who was mentored by Koshland as an undergraduate in 1969 and has remained a colleague and friend for 40 years, said Koshland's ideas were "original, creative and bold." Koshland expected a lot from his students in the lab and in biochemistry class, Tjian said. "He was extremely articulate but also hilariously funny. No one every fell asleep in class," Tjian said. Koshland's sense of humor also spilled over into his position as editor-in-chief of Science - many of the approximately 200 editorials he wrote for the journal were in the form of a dialogue with "Dr. Noitall," a dig at know-it-all scientists.Jingyi Xiang, a postdoctoral researcher who worked with Koshland for the last four years, said Koshland was still working in the lab regularly at 87. Before a recent vacation, Koshland told Xiang that he would be thinking about all of the lab's projects while he was away. "He said that although he's in Lake Tahoe for vacation, his heart is here," Xiang said.Kelly Rae Chi mail@the-scientist.comLinks within this article:Daniel Koshland http://www.berkeley.edu/news/media/releases/2007/07/24_koshland.shtmlLasker Award acceptance comments, 1998 http://www.laskerfoundation.org/awards/library/1998s_pp.shtmlJoseph Goldstein 'http://nobelprize.org/nobel_prizes/medicine/laureates/1985/goldstein-bio.htmlJohn Brauman http://www.stanford.edu/dept/chemistry/faculty/braumanD.E. Koshland, "Application of a Theory of Enzyme Specificity to Protein Synthesis," Proc Natl Acad Sci, Feb. 1958. http://www.the-scientist.com/pubmed/16590179J.B. Stock and D.E. Koshland, "A protein methylesterase involved in bacterial sensing," Proc Natl Acad Sci, Aug. 1978. http://www.the-scientist.com/pubmed/358191Andrew Mesecar http://www.uic.edu/pharmacy/depts/pmch/faculty_sites/Andy.htmA.D. Mesecar et al., "Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences," Science, July 11, 1997. http://www.the-scientist.com/pubmed/9211842H. Black, "Exploring the microbial world," The Scientist, March 10, 2003. http://www.the-scientist.com/article/display/13606Robert Tjian http://www.hhmi.org/research/investigators/tjian.html

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