Synthesis, Characterization, and Nitrogenase-Relevant Reactions of an Iron Sulfide Complex with a Bridging Hydride

被引：27

作者：

Arnet, Nicholas A. ^{[1
]}

Dugan, Thomas R. ^{[2
]}

Menges, Fabian S. ^{[1
]}

Mercado, Brandon Q. ^{[1
]}

Brennessel, William W. ^{[2
]}

Bill, Eckhard ^{[3
]}

Johnson, Mark A. ^{[1
]}

Holland, Patrick L. ^{[1
]}

机构：

[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[2] Univ Rochester, Dept Chem, Rochester, NY 14627 USA

[3] Max Planck Inst Chem Energiekonvers, Mulheim, Germany

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2015年 / 137卷 / 41期

基金：

美国国家卫生研究院;

关键词：

RELAXATION PROTOCOL; ACTIVE-SITE; REDUCTION; H-2; IDENTIFICATION; INTERMEDIATE; SPECTROSCOPY; MOLYBDENUM; MECHANISM; CLEAVAGE;

D O I：

10.1021/jacs.5b06841

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The FeMoco of nitrogenase is an iron-sulfur cluster with exceptional bond-reducing abilities. END OR studies have suggested that E-4, the state that binds and reduces N-2, contains bridging hydrides as part of the active-site iron-sulfide cluster. However, there are no examples of any isolable iron-sulfide cluster with a hydride, which would test the feasibility of such a species. Here, we describe a diiron sulfide hydride complex that is prepared using a mild method involving C-S cleavage of added thiolate. Its reactions with nitrogenase substrates show that the hydride can act as a base or nucleophile and that reduction can cause the iron atoms to bind N-2. These results add experimental support to hydride-based pathways for nitrogenase.

引用

页码：13220 / 13223

页数：4

共 28 条

[1] The Cambridge Structural Database: a quarter of a million crystal structures and rising [J].