Abstract

It is shown that the catalytic center of Thiocapsa roseopersicina remains active after prolonged treatment with cyanide. It was found that the incubation of cyanide-treated hydrogenase in the presence of beta-mercaptoethanol, ferric iron, and sodium sulfide restored the hydrogenase activity in the hydrogen-oxidation reaction in the presence of methylviologen. The process of activity reconstruction depended on time and reached its maximum value (~ 60%) within 30 min at room temperature. In this case, an absorption band at 420 nm appeared in the absorption spectrum of the hydrogenase, which was present in the native hydrogenase and disappeared after treatment with cyanide; this indicated the reconstruction of iron–sulfur clusters. Thus, instead of growing bacteria in the presence of an iron isotope, one can replace ⁵⁶Fe with ⁵⁷Fe in the isolated enzyme, which will allow the use of smaller amounts of ⁵⁷Fe.

中文翻译：

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氰化物抑制后蔷薇硫藻中HydSL氢化酶的重建

摘要

结果表明，在用氰化物长时间处理后，蔷薇硫藻的催化中心仍保持活性。发现在 β-巯基乙醇、三价铁和硫化钠的存在下，氰化物处理的氢化酶在甲基紫精存在下的氢氧化反应中恢复了氢化酶的活性。活动重建的过程取决于时间，并在室温下 30 分钟内达到最大值（~60%）。在这种情况下，氢化酶的吸收光谱中出现了420nm处的吸收带，该吸收带存在于天然氢化酶中，用氰化物处理后消失；这表明铁硫簇的重建。因此，代替在铁同位素存在下培养细菌，人们可以代替⁵⁶分离酶中含有⁵⁷ Fe 的 Fe，这将允许使用更少量的⁵⁷ Fe。