Douglas C. Rees

Douglas Charles "Doug" Rees (born 1952) is an American biochemist, biophysicist, and structural biologist.[1]

Douglas C. Rees
NationalityAmerican
Alma mater
Scientific career
Fields
Institutions
ThesisCrystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A (1980)
Doctoral advisorWilliam Lipscomb
Other academic advisors
  • James Bryant Howard
Websitewww.br.caltech.edu/reesgrp

Rees graduated from Yale University with a bachelor's degree in 1974 and received a PhD in biophysics from Harvard University in 1980.[2] In 1982 he went to the University of California, Los Angeles. In 1989, he became a professor of chemistry at Caltech. There he is Roscoe Gilkey Dickinson Professor and Dean of graduate studies. From 1997 onwards, he has been an investigator of the Howard Hughes Medical Institute. He served as the editor or co-editor of the Annual Review of Biophysics and Biomolecular Structure (20042014).[3][4]

He examines the structure and function of metal-containing proteins, especially nitrogenase in biological nitrogen fixation, and membrane proteins that carry out ATP-dependent transport through membranes (e.g. ABC transporters). To do this, his group uses X-ray crystallography. His interest in nitrogenase began in William Lipscomb's laboratory.

In 2015 he received the FA Cotton Medal, and in 2020 he was awarded the Gregori Aminoff Prize. He is a member of the American Academy of Arts and Sciences, National Academy of Sciences, and was a Sloan Research Fellow.

Writings (selected)

  • Edited with Daniel E. Atkinson, Steven G. Clarke, David S. Barkley: Dynamic models in biochemistry: a workbook of computer simulations using electronic spreadsheets, Benjamin Cummings 1987
  • as editor: Membrane proteins, Amsterdam / Boston: Academic Press, 2003, ISBN 978-0-080-49376-3
  • with JB Howard: Nitrogenase: a nucleotide-dependent molecular switch, Annual Review of Biochemistry, volume 63, 1994, pp. 235–264.
  • with MH Stowell: Structure and stability of membrane proteins, Advances in Protein Chemistry, Volume 46, 1995, pp. 279–311
  • with JB Howard: Structural Basis of Biological Nitrogen Fixation, Chemical Reviews, Volume 96, 1996, pp. 2965–2982
  • with George Feher, et al.: Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer, Science, volume 276, 1997, pp. 812–816
  • Great metalloclusters in enzymology, Annual Review of Biochemistry, Volume 71, 2002, pp. 221–246.
  • with JB Howard: Nitrogenase: standing at the crossroads, Current Opinion in Chemical Biology, Volume 4, 2002, pp. 559–566
  • with F. Akif Tezcan, Chad A. Haynes, Mika Y. Walton, Susana Andrade, Olvier Einsle, James B. Howard: Structural basis of biological nitrogen fixation, Phil. Trans. R. Soc. A, Volume 363, 2005, pp. 971–984
  • with FA Tezcan, JT Kaiser, D. Mustafi, MY Walton, JB Howard: Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein, Science, Volume 309, 2005, pp. 1377–1380
  • with Chris Gandhi: Opening the molecular floodgates, Science, volume 321, 2008, pp. 1166–1167
  • with NS Kadaba, et al.: The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation, Science, volume 321, 2008, pp. 250–253
  • with E. Johnson, O. Lewinson: ABC Transporters: The Power to Change, Nature Reviews Molecular Cell Biology, Volume 10, 2009, pp. 218–227
  • with JB Howard, et al.: Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase, Science, volume 345, 2014, pp. 1620–1623

References

  1. Douglas C. Rees publications from Europe PubMed Central
  2. Career data from Pamela Kalte, et al., American Men and Women of Science, Thomson Gale 2004
  3. Rees, Douglas C. (2004). "Preface by Douglas C. Rees". Annual Review of Biophysics and Biomolecular Structure. 33. doi:10.1146/annurev.bb.33.051304.100011.
  4. Rees, Douglas C. (2012). "Preface". Annual Review of Biophysics. 41. doi:10.1146/annurev-bb-41-050712-100001.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.