James Bryant Howard, professor emeritus of biochemistry at the University of Minnesota Medical School, died suddenly Feb. 13 in Cochiti Lake, New Mexico. He was 79 years old.
Howard was a member of the American Society for Biochemistry and Molecular Biology for over 40 years and served on the editorial board of the Journal of Biological Chemistry from 1986 to 1991.
Born April 25, 1942, in Indianapolis, Howard received his Bachelor of Arts in Chemistry from DePauw University in 1964 before heading west to study at the University of California, Los Angeles. He got his doctorate. in biological chemistry at UCLA in 1968 as one of Alex Glazerfirst graduate students. Howard has often said that the exciting environment of biochemistry at UCLA catalyzed his lifelong passion for protein chemistry, structure, and function.
After a postdoctoral fellowship with Fred Charpentier at UC Berkeley, Howard joined the University of Minnesota Medical School’s biochemistry faculty in 1971, where he remained until becoming emeritus in 2002. Among his notable research accomplishments were his identification of the modified histidine in EF-2 which is the target of ADP-ribosylation by diphtheria toxin (with James Bodley), discovery of the alkylamine-responsive thioester bond in the active site of a2-macroglobulin, and a wide range of studies on nitrogenase proteins, including the determination of the sequence of the nitrogenase iron protein of Azotobacter vinelandii, the identification of the [4Fe:4S] ligands of the clusters and characterizing the chelation and interconversion reactions of the clusters.
A strong believer in the importance of sabbaticals, Howard arranged to visit the Massachusetts Institute of Technology, Harvard, UC Davis, and the National Institutes of Health through this mechanism. I first met him while he was on sabbatical with William Lipscomb at Harvard in 1980-81 to crystallize the protein iron nitrogenase. He convinced me of the importance of a structural approach for the study of nitrogenase which, starting with my postdoctoral position, launched a collaboration of more than 40 years.
For the past two decades – until COVID-19 – this collaboration included annual visits by Jim Howard and his wife, Claralyn, to Pasadena, where I work at the California Institute of Technology. Beyond nitrogenase, Howard had a strong interest in geobiology and interacted extensively with the Caltech community in this area. After becoming emeritus, the Howards moved to New Mexico and his research interests included the isolation and characterization of nitrogen-fixing autotrophs in his home laboratory from year-round seeps in surrounding mesas.
Howard was a real natural philosopher; he enjoyed designing experiments, reviewing results, attending seminars, and discussing what it meant to prove a result. His curiosity was contagious. He focused on the details of experimental design and enjoyed talking with students and postdocs about how to accurately quantify protein concentration, pH temperature dependence, and the importance of force effects. ionic – topics generally considered trivial, but disastrous consequences can result if neglected. A natural skeptic, Howard had a high bar to be convinced, and there was no greater satisfaction than getting to this point with him. Beyond science, he read a lot and loved jazz and art, cycling and sailing, the outdoors. He was an avid student of academia and the big issues of life and society.
Our thoughts are with Claralyn Howard; their daughter, Cathy, and her husband, Tony Grundhauser; granddaughters Emma and Lucy; and Jim’s sister, Aleta Howard, during this difficult time.