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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
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Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components

机译:洞悉利用生物质成分的铜金属酶对纤维素的氧化降解

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摘要

The enzymatic degradation of recalcitrant plant biomass is one of the key industrial challenges of the 21st century. Accordingly, there is a continuing drive to discover new routes to promote polysaccharide degradation. Perhaps the most promising approach involves the application of "cellulase-enhancing factors," such as those from the glycoside hydrolase (CAZy) GH61 family. Here we show that GH61 enzymes are a unique family of copper-dependent oxidases. We demonstrate that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodextrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gal-late. By using electron paramagnetic resonance spectroscopy and single-crystal X-ray diffraction, the active site of GH61 is revealed to contain a type II copper and, uniquely, a methylated histidine in the copper's coordination sphere, thus providing an innovative paradigm in bioinorganic enzymatic catalysis.
机译:难降解植物生物质的酶促降解是21世纪的主要工业挑战之一。因此,存在持续不断的驱动力来发现促进多糖降解的新途径。也许最有前途的方法涉及“纤维素酶增强因子”的应用,例如糖苷水解酶(CAZy)GH61家族的那些。在这里,我们显示GH61酶是铜依赖性氧化酶的独特家族。我们证明铜对于GH61的最大活性是必需的,并且在小分子氧化还原活性辅因子(如抗坏血酸盐和gal-late)的存在下,GH61的纤维糊精和氧化纤维糊精产品的形成得到增强。通过使用电子顺磁共振波谱和单晶X射线衍射,发现GH61的活性位点包含II型铜,并且在铜的配位域中独特地包含甲基化的组氨酸,从而为生物无机酶催化提供了创新的范例。

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