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Structure and Reactivity of an Asymmetric Synthetic Mimic of Nitrogenase Cofactor
Author(s) -
Tanifuji Kazuki,
Sickerman Nathaniel,
Lee Chi Chung,
Nagasawa Takayuki,
Miyazaki Kosuke,
Ohki Yasuhiro,
Tatsumi Kazuyuki,
Hu Yilin,
Ribbe Markus W.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201608806
Subject(s) - nitrogenase , cluster (spacecraft) , reactivity (psychology) , chemistry , catalysis , stereochemistry , cofactor , combinatorial chemistry , enzyme , organic chemistry , nitrogen fixation , nitrogen , alternative medicine , pathology , computer science , programming language , medicine
The Mo nitrogenase catalyzes the ambient reduction of N 2 to NH 3 at its M‐cluster site. A complex metallocofactor with a core composition of [MoFe 7 S 9 C], the M‐cluster, can be extracted from the protein scaffold and used to facilitate the catalytic reduction of CN − , CO, and CO 2 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 [MoFe 5 S 9 ]. 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 C 1 substrates to hydrocarbons suggests the feasibility of developing nitrogenase‐based biomimetic approaches to recycle C 1 waste into fuel products.