Nitrogen reduction by the Fe sites of synthetic [Mo3S4Fe] cubes

Yasuhiro Ohki (), Kenichiro Munakata, Yuto Matsuoka, Ryota Hara, Mami Kachi, Keisuke Uchida, Mizuki Tada, Roger E. Cramer, W. M. C. Sameera, Tsutomu Takayama, Yoichi Sakai, Shogo Kuriyama, Yoshiaki Nishibayashi and Kazuki Tanifuji
Additional contact information
Yasuhiro Ohki: Kyoto University
Kenichiro Munakata: Nagoya University
Yuto Matsuoka: Kyoto University
Ryota Hara: Nagoya University
Mami Kachi: Nagoya University
Keisuke Uchida: Nagoya University
Mizuki Tada: Nagoya University
Roger E. Cramer: University of Hawaii
W. M. C. Sameera: Hokkaido University
Tsutomu Takayama: Daido University
Yoichi Sakai: Daido University
Shogo Kuriyama: The University of Tokyo
Yoshiaki Nishibayashi: The University of Tokyo
Kazuki Tanifuji: Kyoto University

Nature, 2022, vol. 607, issue 7917, 86-90

Abstract: Abstract Nitrogen (N2) fixation by nature, which is a crucial process for the supply of bio-available forms of nitrogen, is performed by nitrogenase. This enzyme uses a unique transition-metal–sulfur–carbon cluster as its active-site co-factor ([(R-homocitrate)MoFe7S9C], FeMoco)1,2, and the sulfur-surrounded iron (Fe) atoms have been postulated to capture and reduce N2 (refs. 3–6). Although there are a few examples of synthetic counterparts of the FeMoco, metal–sulfur cluster, which have shown binding of N2 (refs. 7–9), the reduction of N2 by any synthetic metal–sulfur cluster or by the extracted form of FeMoco10 has remained elusive, despite nearly 50 years of research. Here we show that the Fe atoms in our synthetic [Mo3S4Fe] cubes11,12 can capture a N2 molecule and catalyse N2 silylation to form N(SiMe3)3 under treatment with excess sodium and trimethylsilyl chloride. These results exemplify the catalytic silylation of N2 by a synthetic metal–sulfur cluster and demonstrate the N2-reduction capability of Fe atoms in a sulfur-rich environment, which is reminiscent of the ability of FeMoco to bind and activate N2.

Date: 2022
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41586-022-04848-1 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:607:y:2022:i:7917:d:10.1038_s41586-022-04848-1

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-022-04848-1

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().