Ammonia formation by a thiolate-bridged diiron amide complex as a nitrogenase mimic-Reference-Cited by-同舟云学术

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Ammonia formation by a thiolate-bridged diiron amide complex as a nitrogenase mimic

Published:2013-03-17 Issue:4 Volume:5 Page:320-326
ISSN:1755-4330
Container-title:Nature Chemistry
language:en
Short-container-title:Nature Chem

Author:

Li Yang,Li Ying,Wang Baomin,Luo Yi,Yang Dawei,Tong Peng,Zhao Jinfeng,Luo Lun,Zhou Yuhan,Chen Si,Cheng Fang,Qu Jingping

Publisher

Springer Science and Business Media LLC

Subject

General Chemical Engineering,General Chemistry

Link

http://www.nature.com/articles/nchem.1594.pdf

Reference50 articles.

1. Peters, J. C. & Mehn, M. P. in Activation of Small Molecules: Organometallic and Bioinorganic Perspectives (ed. Tolman, W. B.) 81–119 (Wiley-VCH, 2006).

2. Lee, S. C. & Holm, R. H. The clusters of nitrogenase: synthetic methodology in the construction of weak-field clusters. Chem. Rev. 104, 1135–1158 (2004).

3. Spatzal, T. et al. Evidence for interstitial carbon in nitrogenase FeMo cofactor. Science 334, 940 (2011).

4. Lancaster, K. M. et al. X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron–molybdenum cofactor. Science 334, 974–977 (2011).

5. Barney, B. M. et al. A methyldiazene (HN=N–CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: implications for mechanism. Proc. Natl Acad. Sci. USA 103, 17113–17118 (2006).

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