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Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii

The Carbon Concentration Mechanism (CCM) allows phytoplakton species to accumulate the dissolved inorganic carbon (DIC) necessary for an efficient photosynthesis even under carbon dioxide limitation. In this mechanism of primary importance for diatoms, a key role is played by carbonic anhydrase (CA)...

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Autores principales: Alterio, Vincenzo, Langella, Emma, De Simone, Giuseppina, Monti, Simona Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413181/
https://www.ncbi.nlm.nih.gov/pubmed/25815892
http://dx.doi.org/10.3390/md13041688
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author Alterio, Vincenzo
Langella, Emma
De Simone, Giuseppina
Monti, Simona Maria
author_facet Alterio, Vincenzo
Langella, Emma
De Simone, Giuseppina
Monti, Simona Maria
author_sort Alterio, Vincenzo
collection PubMed
description The Carbon Concentration Mechanism (CCM) allows phytoplakton species to accumulate the dissolved inorganic carbon (DIC) necessary for an efficient photosynthesis even under carbon dioxide limitation. In this mechanism of primary importance for diatoms, a key role is played by carbonic anhydrase (CA) enzymes which catalyze the reversible hydration of CO(2), thus taking part in the acquisition of inorganic carbon for photosynthesis. A novel CA, named CDCA1, has been recently discovered in the marine diatom Thalassiosira weissflogii. CDCA1 is a cambialistic enzyme since it naturally uses Cd(2+) as catalytic metal ion, but if necessary can spontaneously exchange Cd(2+) to Zn(2+). Here, the biochemical and structural features of CDCA1 enzyme will be presented together with its putative biotechnological applications for the detection of metal ions in seawaters.
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spelling pubmed-44131812015-05-07 Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii Alterio, Vincenzo Langella, Emma De Simone, Giuseppina Monti, Simona Maria Mar Drugs Review The Carbon Concentration Mechanism (CCM) allows phytoplakton species to accumulate the dissolved inorganic carbon (DIC) necessary for an efficient photosynthesis even under carbon dioxide limitation. In this mechanism of primary importance for diatoms, a key role is played by carbonic anhydrase (CA) enzymes which catalyze the reversible hydration of CO(2), thus taking part in the acquisition of inorganic carbon for photosynthesis. A novel CA, named CDCA1, has been recently discovered in the marine diatom Thalassiosira weissflogii. CDCA1 is a cambialistic enzyme since it naturally uses Cd(2+) as catalytic metal ion, but if necessary can spontaneously exchange Cd(2+) to Zn(2+). Here, the biochemical and structural features of CDCA1 enzyme will be presented together with its putative biotechnological applications for the detection of metal ions in seawaters. MDPI 2015-03-25 /pmc/articles/PMC4413181/ /pubmed/25815892 http://dx.doi.org/10.3390/md13041688 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Alterio, Vincenzo
Langella, Emma
De Simone, Giuseppina
Monti, Simona Maria
Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title_full Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title_fullStr Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title_full_unstemmed Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title_short Cadmium-Containing Carbonic Anhydrase CDCA1 in Marine Diatom Thalassiosira weissflogii
title_sort cadmium-containing carbonic anhydrase cdca1 in marine diatom thalassiosira weissflogii
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413181/
https://www.ncbi.nlm.nih.gov/pubmed/25815892
http://dx.doi.org/10.3390/md13041688
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