嗜热菌 HB27 漆酶的稳定性/活性权衡。
Stability/activity tradeoffs in Thermusthermophilus HB27 laccase.
机构信息
Beckman Institute, California Institute of Technology, Pasadena, CA, 91125, USA.
出版信息
J Biol Inorg Chem. 2020 Mar;25(2):233-238. doi: 10.1007/s00775-020-01754-7. Epub 2020 Jan 22.
Abstract
We report the temperature dependence of the formal potential of type 1 copper (Cu) in Thermusthermophilus HB27 laccase. Employing Ru(NH)(bpy) (0.505 vs. NHE) as the redox titrant, we found that the Cu potential decreased from approximately 480 to 420 mV (vs. NHE) as the temperature was raised from 20 to 65 °C. Of importance is that the ΔS° of - 120 J mol K is substantially more negative than those for other blue copper proteins. We suggest that the highly unfavorable reduction entropy is attributable to Cu inaccessibility to the aqueous medium. Although the active site residues are buried, which is critical for maintaining thermostability, the flexibility around Cu is maintained, allowing enzyme activity at ambient temperature.
摘要
我们报告了嗜热菌 HB27 漆酶中 1 型铜（Cu）的形式电势随温度的变化关系。我们使用 Ru(NH)(bpy)（相对于 NHE 为 0.505）作为氧化还原滴定剂，发现 Cu 电势随温度从 20°C 升高到 65°C 而从约 480 mV 降低到 420 mV（相对于 NHE）。重要的是，与其他蓝铜蛋白相比，ΔS°值为−120 J mol K，明显更负。我们认为，Cu 难以进入水相是导致还原熵非常不利的原因。尽管活性位点残基被掩埋，这对于维持热稳定性至关重要，但 Cu 周围的柔韧性得以保持，从而使酶在环境温度下具有活性。
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