{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tanifuji K"],"funding":["Kyoto University","Takeda Science Foundation","Ministry of Education, Culture, Sports, Science and Technology","Basic Energy Sciences","Tatematsu Foundation","NIGMS NIH HHS","National Science Foundation"],"pagination":["e202200384"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9547968"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(19)"],"pubmed_abstract":["Nitrogenase employs a sophisticated electron transfer system and a Mo-Fe-S-C cofactor, designated the M-cluster [(cit)MoFe<sub>7</sub> S<sub>9</sub> C]), to reduce atmospheric N<sub>2</sub> to bioaccessible NH<sub>3</sub> . 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 [Fe<sub>6</sub> S<sub>9</sub> (SEt)<sub>2</sub> ]<sup>4-</sup> . Here, we demonstrate the utility of an asymmetric Mo-Fe-S cluster [Cp*MoFe<sub>5</sub> S<sub>9</sub> (SH)]<sup>3-</sup> as an alternative artificial cofactor upon incorporation into the cofactor-free nitrogenase scaffold. The resultant semi-artificial enzyme catalytically reduces C<sub>2</sub> H<sub>2</sub> to C<sub>2</sub> H<sub>4</sub> , and CN<sup"],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Incorporation of an Asymmetric Mo-Fe-S Cluster as an Artificial Cofactor into Nitrogenase."],"pmcid":["PMC9547968"],"funding_grant_id":["19H02733","21K20557","23000007","20K21207","21H00021","P30 GM133894","CHE-1904131","R01 GM067626","DE-AC02-76SF00515"],"pubmed_authors":["Ribbe MW","Hu Y","Tanifuji K","Solomon JB","Nagasawa T","Jasniewski AJ","Lee CC","Hedman B","Ohki Y","Tatsumi K","Hodgson KO"],"additional_accession":[]},"is_claimable":false,"name":"Incorporation of an Asymmetric Mo-Fe-S Cluster as an Artificial Cofactor into Nitrogenase.","description":"Nitrogenase employs a sophisticated electron transfer system and a Mo-Fe-S-C cofactor, designated the M-cluster [(cit)MoFe<sub>7</sub> S<sub>9</sub> C]), to reduce atmospheric N<sub>2</sub> to bioaccessible NH<sub>3</sub> . 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 [Fe<sub>6</sub> S<sub>9</sub> (SEt)<sub>2</sub> ]<sup>4-</sup> . Here, we demonstrate the utility of an asymmetric Mo-Fe-S cluster [Cp*MoFe<sub>5</sub> S<sub>9</sub> (SH)]<sup>3-</sup> as an alternative artificial cofactor upon incorporation into the cofactor-free nitrogenase scaffold. The resultant semi-artificial enzyme catalytically reduces C<sub>2</sub> H<sub>2</sub> to C<sub>2</sub> H<sub>4</sub> , and CN<sup","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-28T01:35:38.111Z","creation":"2025-04-06T10:18:57.185Z"},"accession":"S-EPMC9547968","cross_references":{"pubmed":["35925843"],"doi":["10.1002/cbic.202200384"]}}