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Photograph: University of Wisconsin, Madison, Biochemistry Department

Metallobiochemistry lost one of its greatest figures with the passing of Helmut Beinert on 21 December 2007, at the age of 94. Beinert was a native of Germany and received his education there. His research career was spent primarily at the Institute for Enzyme Research at the University of Wisconsin–Madison (1950–1985), where he rose to the rank for Professor of Biochemistry, and then at the Medical College of Wisconsin (1985–1994). Thereafter, he returned to Madison as Professor Emeritus and continued his active research career until his death. While Beinert’s activities ranged over a number of areas in biochemistry, he is best known and will be long remembered for his seminal role in the development of the field of iron-sulfur biochemistry. This work began with studies of mitochondrial electron transport enzymes and included pioneering use of EPR spectroscopy in the study of metalloproteins and the discovery (with Sands) of the famous “g = 1.94-type” spectrum of reduced proteins. His later work encompassed isolation and biochemical and physical characterization of a number of different iron-sulfur proteins. Representative of Beinert’s remarkable research scholarship is his collaborative body of work on cytosolic and mitochondrial aconitase. All who knew him appreciated his unique scientific acumen and his broad grasp of and devotion to biochemical science. Beinert was the recipient of a number of awards and honorary degrees and was a member for the US National Academy of Sciences. Perhaps the most fulfilling recognition of his accomplishments is the widely held accolade as the “father of iron-sulfur biochemistry,” the single figure most responsible for the growth of this subject from scientific obscurity to prosperity.

14 February 2008