ADVERTISEMENT
2 /3 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Physical Chemistry

Nitrogenase Structure Solved With Carbon Monoxide Bound

Substrate analog displaces sulfur from the nitrogen-fixing enzyme’s FeMo cofactor

by Jyllian Kemsley
September 29, 2014 | APPEARED IN VOLUME 92, ISSUE 39

[+]Enlarge
Credit: Thomas Spatzal/Caltech
CO displaces a sulfur atom in the FeMo cofactor of nitrogenase.
09239-scicon-nitrogenasecxd_18198989-690.jpg
Credit: Thomas Spatzal/Caltech
CO displaces a sulfur atom in the FeMo cofactor of nitrogenase.

A crystal structure of the enzyme nitrogenase, which some microorganisms use to turn nitrogen into useful ammonia, has at last been captured with a substrate analog bound to its catalytic metal cluster. The structural snapshot reveals that CO can displace a S atom from the enzyme’s FeMo cofactor, a cagelike assembly of Fe, S, C, and Mo, reports a team led by Thomas Spatzal and Douglas C. Rees of Caltech (Science 2014, DOI: 10.1126/science.1256679). Researchers have struggled to unravel how nitrogenase does its N2-reduction chemistry, which could point to better ways to make NH3 than the energy-intensive Haber-Bosch process. CO is isoelectronic with N2 and is a reversible nitrogenase inhibitor. The molecule’s binding to two iron atoms in the cofactor resembles N2 binding on the surface of the iron catalyst used in the Haber-Bosch process, the researchers note.

X

Article:

This article has been sent to the following recipient:

Leave A Comment

*Required to comment