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Double‐Cubane [8Fe9S] Clusters: A Novel Nitrogenase‐Related Cofactor in Biology
Author(s) -
Jeoung JaeHun,
Martins Berta M.,
Dobbek Holger
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000016
Subject(s) - cubane , cofactor , nitrogenase , enzyme , chemistry , electron transfer , electron transport chain , corrinoid , ligand (biochemistry) , iron–sulfur cluster , stereochemistry , oxidoreductase , biochemistry , crystallography , photochemistry , nitrogen fixation , dna , receptor , organic chemistry , crystal structure , methyltransferase , methylation , nitrogen
Three different types of electron‐transferring metallo‐ATPases are able to couple ATP hydrolysis to the reduction of low‐potential metal sites, thereby energizing an electron. Besides the Fe‐protein known from nitrogenase and homologous enzymes, two other kinds of ATPase with different scaffolds and cofactors are used to achieve a unidirectional, energetic, uphill electron transfer to either reduce inactive Co‐corrinoid‐containing proteins (RACE‐type activators) or a second iron‐sulfur cluster‐containing enzyme of a unique radical enzymes family (archerases). We have found a new cofactor in the latter enzyme family, that is, a double‐cubane cluster with two [4Fe4S] subclusters bridged by a sulfido ligand. An enzyme containing this cofactor catalyzes the ATP‐dependent reduction of small molecules, including acetylene. Thus, enzymes containing the double‐cubane cofactor are analogous in function and share some structural features with nitrogenases.