Incorporation of an Asymmetric Mo−Fe−S Cluster as an Artificial Cofactor into Nitrogenase. (25th August 2022)

• Record Type: Journal Article
• Authors: Tanifuji, Kazuki; Jasniewski, Andrew J.; Lee, Chi Chung; Solomon, Joseph B.; Nagasawa, Takayuki; Ohki, Yasuhiro; Tatsumi, Kazuyuki; Hedman, Britt; Hodgson, Keith O.; Hu, Yilin; Ribbe, Markus W.
• Is Part Of: Chembiochem. Volume 23:Number 19(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-08-25
• Subjects: artificial enzymes -- C1 substrate reduction -- hydrocarbons -- nitrogenases -- synthetic Mo−Fe−S clusters; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202200384
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Nitrogenase employs a sophisticated electron transfer system and a Mo−Fe−S−C cofactor, designated the M‐cluster [(cit)MoFe7 S9 C]), to reduce atmospheric N2 to bioaccessible NH3 . Previously, we have shown that the cofactor‐free form of nitrogenase can be repurposed as a protein scaffold for the incorporation of a synthetic Fe−S cluster [Fe6 S9 (SEt)2 ] 4− . Here, we demonstrate the utility of an asymmetric Mo−Fe−S cluster [Cp*MoFe5 S9 (SH)] 3− as an alternative artificial cofactor upon incorporation into the cofactor‐free nitrogenase scaffold. The resultant semi‐artificial enzyme catalytically reduces C2 H2 to C2 H4, and CN − into short‐chain hydrocarbons, yet it is clearly distinct in activity from its [Fe6 S9 (SEt)2 ] 4− ‐reconstituted counterpart, pointing to the possibility to employ molecular design and cluster synthesis strategies to further develop semi‐artificial or artificial systems with desired catalytic activities. Abstract : Incorporation of a synthetic asymmetric Mo−Fe−S cluster, [Cp*MoFe5 S9 (SH)] 3−, into the active site of the cofactor‐free nitrogenase scaffold results a semi‐artificial enzyme that catalytically reduces C2 H2 to C2 H4, and CN − into short‐chain hydrocarbons.