Douglas C. Rees

Dr. Douglas C. Rees

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Research Focus & Metrics

Academic Career Length

28Years (1999-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 March 2009 in Nature Reviews Molecular Cell Biology
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DRDouglas C. Rees
Douglas C. Rees
EJEric Johnson
Eric Johnson
OLOded Lewinson
Oded Lewinson

15 June 2020 in Chemical Reviews
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OEOliver Einsle
Oliver Einsle
DRDouglas C. Rees
Douglas C. Rees

1 October 2011 in Structure
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Journal Article
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EHElizabeth S. Haswell
Elizabeth S. Haswell
RPRob Phillips
Rob Phillips
DRDouglas C. Rees
Douglas C. Rees

26 September 2014 in Science
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TSThomas Spatzal
Thomas Spatzal
KPKathryn A. Perez
Kathryn A. Perez
OEOliver Einsle
Oliver Einsle
JHJames B. Howard
James B. Howard
DRDouglas C. Rees
Douglas C. Rees
Making nitrogen available for biosynthesis: Nitrogen gas (N 2 ) is abundant in Earth's atmosphere; however, it must be converted into a bioavailable form before it can be incorporated into biomolecules. The enzyme nitrogenase, which is made up of two metalloproteins, converts N 2 into bioavailable ammonia. One of these, the MoFe-protein, contains a complex metal center, the FeMo cofactor, where the triple N 2 bond is reduced. Understanding how nitrogenase achieves the reduction of N 2 has been a long-term goal. Spatzal et al. present the structure of MoFe-protein bound to carbon monoxide (see the Perspective by Hogbom). Although this is an inhibitor rather than the natural substrate, the structure gives insight into how the FeMo metallocluster rearranges to achieve substrate reduction. Science , this issue p. 1620

5 April 2005 in Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences
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DRDouglas C. Rees
Douglas C. Rees
FTF Akif Tezcan
F Akif Tezcan
CHChad A Haynes
Chad A Haynes
MWMika Y Walton
Mika Y Walton
SASusana Andrade
Susana Andrade
JHJames B Howard
James B Howard
Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor that provides the active site for substrate reduction, and the Fe-protein that couples ATP hydrolysis to electron transfer. An overview of the nitrogenase system is presented that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions. Although the mechanism of ammonia formation by nitrogenase remains enigmatic, mechanistic inferences motivated by recent developments in the areas of nitrogenase biochemistry, spectroscopy, model chemistry and computational studies are discussed within this structural framework.

1 October 2000 in Current Opinion in Chemical Biology
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DRDouglas C. Rees
Douglas C. Rees
JHJames B Howard
James B Howard