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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond
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Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond

机译：结构和催化特性人类的耐热、耐酸作用变体碳酸酐酶II包含一个工程二硫键

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摘要

The carbonic anhydrases (CAs) are a family of mostly zinc metalloenzymes that catalyze the reversible hydration of CO2 to bicarbonate and a proton. Recently, there has been industrial interest in utilizing CAs as biocatalysts for carbon sequestration and biofuel production. The conditions used in these processes, however, result in high temperatures and acidic pH. This unfavorable environment results in rapid destabilization and loss of catalytic activity in CAs, ultimately resulting in cost-inefficient high-maintenance operation of the system. In order to negate these detrimental industrial conditions, cysteines at residues 23 (Ala23Cys) and 203 (Leu203Cys) were engineered into a wild-type variant of human CA II (HCAII) containing the mutation Cys206Ser. The X-ray crystallographic structure of the disulfide-containing HCAII (dsHCAII) was solved to 1.77 ? resolution and revealed that successful oxidation of the cysteine bond was achieved while also retaining desirable active-site geometry. Kinetic studies utilizing the measurement of 18O-labeled CO2 by mass spectrometry revealed that dsHCAII retained high catalytic efficiency, and differential scanning calorimetry showed acid stability and thermal stability that was enhanced by up to 14 K compared with native HCAII. Together, these studies have shown that dsHCAII has properties that could be used in an industrial setting to help to lower costs and improve the overall reaction efficiency.
机译：碳酸脱水酶(CAs)是一个家庭的主要是锌近年,催化可逆水合二氧化碳碳酸氢盐和质子。利用中科院作为生物催化剂的兴趣固碳和生物燃料生产。然而,环境中使用这些过程导致高温和酸性博士不利的环境导致快速不稳定的催化活性和损失中科院,最终导致cost-inefficient奢侈的操作系统。以否定这些有害的工业条件,半胱氨酸残基23日(Ala23Cys)和203 (Leu203Cys)改造成一个野生型变异的人类CA II (HCAII)包含变异Cys206Ser。晶体的结构disulfide-containing HCAII (dsHCAII)解决1.77吗?半胱氨酸的氧化债券得以实现,同时也保持理想的活性部位的几何形状。利用测量的动力学研究18 o-labeled二氧化碳通过质谱显示dsHCAII保留催化效率高,和差示扫描量热法酸稳定性和热稳定性增强14 K与本机HCAII相比。这些研究表明,dsHCAII属性可用于一个吗帮助降低成本和工业设置提高整体反应效率。

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