The multiple roles of carbonic anhydrase in calcium carbonate mineralization
Autor: | Carlos Rodriguez-Navarro, Encarnación Ruiz-Agudo, Kerstin Elert, Alejandro Burgos-Cara, Krzysztof Kudłacz, Aurelia Ibañez-Velasco, Cristina Ruiz-Agudo, Özlem Cizer |
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Rok vydání: | 2019 |
Předmět: |
Calcite
chemistry.chemical_classification biology Chemistry chemistry.chemical_element 02 engineering and technology General Chemistry Mineralization (soil science) Calcium 010402 general chemistry 021001 nanoscience & nanotechnology Condensed Matter Physics Fibril 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Calcium carbonate Enzyme Carbonic anhydrase Biophysics biology.protein General Materials Science 0210 nano-technology Biomineralization |
Popis: | Carbonic anhydrase (CA), a ubiquitous enzyme that catalyzes the reversible hydration of CO2, is known to be involved in the formation of CaCO3 biominerals and is currently used for biomimetic CO2 mineral sequestration. However, its specific role(s) in calcium carbonate (bio)mineralization is poorly understood. Here we show that CA catalyzes the formation of the reactive precursors (i.e., HCO3− and CO32− ions) required for mineralization, accelerates the precipitation of metastable amorphous calcium carbonates and their solution-mediated conversion into crystalline calcite, which grows via a non-classical nanoparticle aggregation mechanism that facilitates CA occlusion. Ca+ and CO32− ions promote the partial unfolding and oligomerization of CA, resulting in fibril- and sheet-like supramolecular assemblies that template nanostructured calcium carbonate crystallization. By losing its catalytic activity following the observed conformational changes, CA elicits a mechanism for arresting calcium carbonate mineralization. Our results show that CA can play multiple, until now unrecognized, critical roles, namely, as an enzyme and structural protein in CaCO3 biomineralization and also helps to explain the observed loss of enzymatic activity during ex situ CO2 mineral sequestration. |
Databáze: | OpenAIRE |
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