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[FeFe]-hydrogenases catalyze the protons/hydrogen interconversion through a unique di-iron active site consisting of three CO and two CN ligands, and a non-protein SCH 2 XCH 2 S (X=N or O) dithiolate bridge. Site assembly requires two “Radical-S-adenosylmethionine (SAM or AdoMet)” iron–sulfur enzymes, HydE and HydG, and one GTPase, HydF. The sequence homology between HydG and ThiH,...
Spore photoproduct lyase (SPL) is a “Radical-SAM” repair enzyme which catalyzes the cleavage of spore photoproduct (SP, 5-thyminyl-5,6-dihydrothymine), a specific lesion found in bacterial spore DNA, to thymine monomers by a free-radical mechanism. The enzyme requires S-adenosyl-l-methionine (SAM) and a [4Fe–4S] cluster for activity. SPL from Bacillus subtilis has been difficult to isolate and characterize...
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