Journal Article Structure and Reactivity of an Asymmetric Synthetic Mimic of Nitrogenase Cofactor

Tanifuji, Kazuki  ,  Sickerman, Nathaniel  ,  Lee, Chi Chung  ,  Nagasawa, Takayuki  ,  Miyazaki, Kosuke  ,  Ohki, Yasuhiro  ,  Tatsumi, Kazuyuki  ,  Hu, Yilin  ,  Ribbe, Markus W.

55 ( 50 )  , pp.15633 - 15636 , 2016-12-12 , Wiley
ISSN:1433-7851
Description
The Mo nitrogenase catalyzes the ambient reduction of N2 to NH3 at its M-cluster site. A complex metallocofactor with a core composition of [MoFe7S9C], the M-cluster, can be extracted from the protein scaffold and used to facilitate the catalytic reduction of CN−, CO, and CO2 into hydrocarbons in the isolated state. Herein, we report the synthesis, structure, and reactivity of an asymmetric M-cluster analogue with a core composition of [MoFe5S9]. This analogue, referred to as the Mo-cluster, is the first synthetic example of an M-cluster mimic with Fe and Mo positioned at opposite ends of the cluster. Moreover, the ability of the Mo-cluster to reduce C1 substrates to hydrocarbons suggests the feasibility of developing nitrogenase-based biomimetic approaches to recycle C1 waste into fuel products.
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