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CuI and H2O2 Inactivate and FeII Inhibits [Fe]‐Hydrogenase at Very Low Concentrations

[Fe]‐Hydrogenase (Hmd) catalyzes reversible hydride transfer from H2. It harbors an iron‐guanylylpyridinol as a cofactor with an FeII that is ligated to one thiolate, two COs, one acyl‐C, one pyridinol‐N, and solvent. Here, we report that CuI and H2O2 inactivate Hmd (half‐maximal rates at 1 μM CuI and 20 μM H2O2) and that FeII inhibits the enzyme with very high affinity (Ki=40 nM). Infrared and EPR studies together with competitive inhibition studies with isocyanide indicated that CuI exerts its inhibitory effect most probably by binding to the active site iron‐thiolate ligand. Using the same methods, it was found that H2O2 binds to the active‐site iron at the solvent‐binding site and oxidizes FeII to FeIII. Also it was shown that FeII reversibly binds away from the active site iron, with binding being competitive to the organic hydride acceptor; this inhibition is specific for FeII and is reminiscent of that for the [FeFe]‐hydrogenase second iron, which specifically interacts with H2.