DOI: 10.1126/science.1256679. Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

10.1126/science.1256679

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

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

Bibliography

Spatzal, T., Perez, K. A., Einsle, O., Howard, J. B., & Rees, D. C. (2014). Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase. Science, 345(6204), 1620â1623.

Authors 5

Thomas Spatzal (first)
Kathryn A. Perez (additional)
Oliver Einsle (additional)
James B. Howard (additional)
Douglas C. Rees (additional)

References 43 Referenced 376

Dates

Type	When
Created	10 years, 11 months ago (Sept. 25, 2014, 3:08 p.m.)
Deposited	1 year, 7 months ago (Jan. 10, 2024, 4:22 p.m.)
Indexed	1 week, 4 days ago (Aug. 26, 2025, 2:42 a.m.)
Issued	10 years, 11 months ago (Sept. 26, 2014)
Published	10 years, 11 months ago (Sept. 26, 2014)
Published Print	10 years, 11 months ago (Sept. 26, 2014)

Funders 0

None

BibTeX

@article{Spatzal_2014, title={Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase}, volume={345}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1256679}, DOI={10.1126/science.1256679}, number={6204}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Spatzal, Thomas and Perez, Kathryn A. and Einsle, Oliver and Howard, James B. and Rees, Douglas C.}, year={2014}, month=sep, pages={1620–1623} }

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