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An '''azadithiolate cofactor''' is an [[anion]] with the formula NH(CH<sub>2</sub>S)<sub>2</sub><sup>2−</sup>. It is used as a [[cofactor (biochemistry)|cofactor]] in the [FeFe] [[hydrogenase]]s, [[enzymes|bacterial enzymes]] responsible for the reversible reduction of 2 H<sup>+</sup> to H<sub>2</sub>.<ref>{{cite journal | last1 = Berggren, | first1 = G., | last2 = Adamska, | first2 = A., | last3 = Lambertz, | first3 = C., | last4 = Simmons, | first4 = T. R., | last5 = Esselborn, | first5 = J., | last6 = Atta, | first6 = A., | last7 = Gambarelli, | first7 = S., | last8 = Mouesca, | first8 = J.-M., | last9 = Reijerse, | first9 = E., | last10 = Lubitz, | first10 = W., | last11 = Happe, | first11 = T., | last12 = Artero, | first12 = V., | last13 = Fontecave, | first13 = M. "| year = 2013 | title = Biomimetic assembly and activiation of [FeFe]-hydrogenases" ''| url = | journal = Nature'' 2013,| vol.volume = 499, | issue = | page = 66 {{DOI| doi = 10.1038/nature12239 }}</ref> As a cofactor, the two [[thiol|thiolate]] [[functional group]]s are bound to each of the two irons in the [[active site]] of the enzyme in a [[bridging ligand|bridging fashion]]. The [[amine]] functional group serves as an [[acid-base reaction|acid/base]] to transfer H<sup>+</sup> from the solution to the active site. The proton transfer function of this cofactor is of great importance to the activity of the hydrogenase enzyme, as H<sub>2</sub> evolution will not occur if the amine is not present.
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