Synthesis of Cp*-supported metal-sulfur clusters as functional analogues of the active site of nitrogenase

2018 Fiscal Year Final Research Report

• Project/Area Number: 16H04116
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Inorganic chemistry
• Research Institution: Nagoya University
• Principal Investigator: Ohki Yasuhiro 名古屋大学, 理学研究科, 准教授 (10324394)
• Project Period (FY): 2016-04-01 – 2019-03-31
• Keywords: 窒素固定化 / ニトロゲナーゼ / 金属-硫黄クラスター / モリブデン

Outline of Final Research Achievements

Inorganic components consisting of multiple transition metals and sulfur atoms are designated as metal-sulfur clusters, which are essential for various biological functions. The largest biological metal-sulfur cluster thus far structurally identified is the nitrogenase FeMo-cofactor, which catalyzes the reduction of N2 into NH3 under physiological conditions. Although various metal-sulfur clusters structurally relevant to FeMo-cofactor have been synthesized over the years, their use in the activation of N2 has proven challenging to realize, and even the FeMo-cofactor extracted from the protein to organic solvents has not been found to reduce N2. In this research project, we synthesized a series of Cp* (C5Me5)-supported cubic [Mo3S4M] clusters, and demonstrated the activation of N2 and its conversion into NH3 and N2H4 on the [Mo3S4Ti] variant. This result represents an initial step toward modeling the reducing function of the FeMo-cofactor.

Free Research Field

錯体化学、生物無機化学、有機金属化学

Academic Significance and Societal Importance of the Research Achievements

本研究では、多数の金属原子と硫黄原子を集めた「金属-硫黄クラスター」分子を用いて、N2を捕捉し還元できることを世界で初めて実証した。この研究をさらに発展させることで、酵素タンパク中で金属-硫黄クラスターがどのようにN2を捕捉し還元するかを明らかにすることや、酵素のN2還元機能を人工的に再現することが可能になると期待される。