Richard H. Holm

Richard Hadley Holm (born September 24, 1933 in Boston, Massachusetts), also known as R. H. Holm, is an American inorganic chemist.

This article is about an inorganic chemist. For the CIA officer, see Dick Holm.

Holm received his Ph.D. from the Massachusetts Institute of Technology in 1959 under the direction of F. Albert Cotton.[1][2] After the completion of his degree, he joined the chemistry faculty at Harvard University. He has been on the faculties of the University of Wisconsin–Madison, Massachusetts Institute of Technology, and Stanford University. He is the Higgins Professor of Chemistry at Harvard.

His accomplishments have been honored with numerous awards including the National Academy of Sciences Award in Chemical Sciences.[3] and the F.A. Cotton Medal for Excellence in Chemical Research of the American Chemical Society in 2005. He is a member of National Academy of Sciences and the American Academy of Arts and Sciences.

Holm's research encompasses synthetic, structural, and reactivity aspects of transition element chemistry. He is best known for the preparations of the first synthetic analogs of the active sites of iron-sulfur proteins.[4] These discoveries were significant in the development of bioinorganic chemistry. He continues his work in the field of iron-sulfur clusters today, examining the active sites of the enzymes nitrogenase and carbon monoxide dehydrogenase. Additionally, his interests include the biomimetic chemistry of molybdenum- and tungsten-containing oxo-transferases.

See also

References
  1. Chemical genealogy, Michigan State U. chemistry dept.
  2. Stanford Chemistry Dept. History 1977–2000: Professors, Brief Biographical Summaries Archived 2012-02-12 at the Wayback Machine, Stanford U.
  3. National Academy of Sciences. NAS Award in Chemical Sciences Archived 2010-12-29 at the Wayback Machine, Accessed on October 18, 2007.
  4. Herskovitz, T.; Averill, B. A.; Holm, R. H.; Ibers, J. A.; Phillips, W. D. & Weiher, J. F. (1972), "Structure and properties of a synthetic analogue of bacterial iron-sulfur proteins", Proceedings of the National Academy of Sciences, 69 (9): 2437–2441, doi:10.1073/pnas.69.9.2437, PMC 426959, PMID 4506765.



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