Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus

Characterization of Biomimetic Cofactors According to Stability, Redox Potentials, and Enzymatic Conversion by NADH Oxidase from Lactobacillus pentosus
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DOI:
10.1002/cbic.201700258
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发表时间:
2017-10-05
期刊:
影响因子:
3.2
通讯作者:
Sieber, Volker
Sieber, Volker
中科院分区:
生物学3区
文献类型:
--
作者:
Nowak, Claudia;Pick, Andre;Sieber, Volker

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氧化还原酶是一种有吸引力的生物催化剂,可以将非手性底物转化为更高价值的产物,但它们在很大程度上也依赖于烟酰胺辅助因子。最近,仿生烟酰胺衍生物作为天然辅助因子的低成本替代品而受到关注。然而,仿生学的回收利用仍然具有挑战性,因为机会有限。在这里,我们对各种仿生辅因子的稳定性和氧化还原电位进行了表征,以找到天然辅因子的最佳替代品。进一步扩大了戊酸乳杆菌(Lactobacillus pentosus, LpNox) NADH氧化酶的辅因子谱,并与不同小分子催化剂的酶活性进行了比较。因此,我们成功地确定了几种氧化仿生物再生的策略。
Oxidoreductases are attractive biocatalysts that convert achiral substrates into products of higher value, but they are also for the most part dependent on nicotinamide cofactors. Recently, biomimetic nicotinamide derivatives have received attention as less costly alternatives to natural cofactors. However, recycling of biomimetics is still challenging because there are only limited opportunities. Here, we have characterized various biomimetic cofactors with regard to stability and redox potentials to find the best alternative to natural cofactors. Further, the cofactor spectrum of NADH oxidase from Lactobacillus pentosus (LpNox) could be expanded, and the enzymatic activity was also compared to activities with different small-molecule catalysts. As a result, we succeeded in identifying several strategies for regeneration of oxidized biomimetics.