2.8.1.8	4Fe-4S-center	-	739557	
2.8.1.8	4Fe-4S-center	the enzyme LipA harbors two [4Fe-4S] clusters that are essential for its activity	737720	
2.8.1.8	S-adenosyl-L-methionine	-	711217, 737696, 739557	
2.8.1.8	[4Fe-4S]-center	-	760401	
2.8.1.8	[4Fe-4S]-center	LipA contains two [4Fe-4S] clusters, one of them is degraded during turnover, limiting LipA to one turnover in vitro. The iron-sulfur (Fe-S) cluster carrier protein NfuA, the bacterial ortholog of NFU1, efficiently reconstitutes the auxiliary cluster during LipA catalysis in a step that is not rate-limiting	762468	
2.8.1.8	[4Fe-4S]-center	the ground state of the two FeS clusters, both in the [4Fe4S]2+ oxidation state, is a singlet state with antiferromagnetically coupled high-spin Fe ions. There is a large variation of the energies of the various broken-symmetry states, up to 40 kJ/mol. For the two S-insertion reactions, the highest energy barrier is found for the hydrogen-atom abstraction from the octanoyl substrate by 5'-dA radical. The formation of 5'-dA radical shows an energy barrier of 6 kJ/mol for the first S-insertion reaction and no barrier for the second S-insertion reaction. Thehe first S ion attack on the C6 radical of octanoyl takes place directly by the transfer of the H6 from the substrate to 5'-dA radical, whereas for the second S-insertion reaction, a C8 radical intermediate is formed with a rate-limiting barrier of 71 kJ/mol	761530