ArticleActa crystallographica. Section D, Biological crystallography2013
Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- A reverse vaccinology approach on transmembrane carbonic anhydrases from Plasmodium species as vaccine candidates for malaria prevention.Malaria journal · 2022Article
- Crystal Structure of a Highly Thermostable α-Carbonic Anhydrase from Persephonella marina EX-H1.Molecules and cells · 2019Article
- Crystal structure and chemical inhibition of essential schistosome host-interactive virulence factor carbonic anhydrase SmCA.Communications biology · 2019Article
- In Silico Designing of an Industrially Sustainable Carbonic Anhydrase Using Molecular Dynamics Simulation.ACS omega · 2016Article
- The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis.Biochemistry · 2016Article
- Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration.Scientific reports · 2016Article
- Acidic sweep gas with carbonic anhydrase coated hollow fiber membranes synergistically accelerates CO2 removal from blood.Acta biomaterialia · 2015Article
- Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Thermostable Carbonic Anhydrases in Biotechnological Applications.International journal of molecular sciences · 2015Review
- Kinetics of CO2 exchange with carbonic anhydrase immobilized on fiber membranes in artificial lungs.Journal of materials science. Materials in medicine · 2015Article
- Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.The FEBS journal · 2015Article
- Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II.Archives of biochemistry and biophysics · 2013Article
- Carbonic anhydrases and their biotechnological applications.Biomolecules · 2013Article
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5 authors.
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Abstract
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 Å 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 (18)O-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.
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