Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Molybdenum (Mo-) nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. This group contains the beta subunit of the MoFe protein. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction.
Comment:MoFe protein is an alpha2beta2 heterotetramer. Each alphabeta dimer has an iron-sulfur P cluster which bridges the alpha and beta subunit.
Structure:2AFK; Azotobacter vinelandii, MoFe protein/Av1 alpha2beta2 heterotetramer showing beta subunit (chains B and D) contacts with P-clusters at 3.5 A
Jiyao W et al.(2023). "The conserved domain database in 2023.",