Single enzyme direct biomineralization of CdSe and CdSe-CdS core-shell quantum dots

Yang, Zhou, Lu, Li, Kiely, Christopher J. ORCID: https://orcid.org/0000-0001-5412-0970, Berger, Bryan W. and McIntosh, Steven 2017. Single enzyme direct biomineralization of CdSe and CdSe-CdS core-shell quantum dots. ACS Applied Materials and Interfaces 9 (15) , pp. 13430-13439. 10.1021/acsami.7b00133

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Abstract

Biomineralization is the process by which biological systems synthesize inorganic materials. Herein, we demonstrate an engineered cystathionine γ-lyase enzyme, smCSE that is active for the direct aqueous phase biomineralization of CdSe and CdSe-CdS core-shell nanocrystals. The nanocrystals are formed in an otherwise unreactive buffered solution of Cd acetate and selenocystine through enzymatic turnover of the selenocystine to form a reactive precursor, likely H2Se. The particle size of the CdSe core nanocrystals can be tuned by varying the incubation time to generated particle sizes between 2.74 ± 0.63 nm and 4.78 ± 1.16 nm formed after 20 min and 24 h of incubation, respectively. Subsequent purification and introduction of l-cysteine as a sulfur source facilitates the biomineralization of a CdS shell onto the CdSe cores. The quantum yield of the resulting CdSe-CdS core-shell particles is up to 12% in the aqueous phase; comparable to that reported for more traditional chemical synthesis routes for core-shell particles of similar size with similar shell coverage. This single-enzyme route to functional nanocrystals synthesis reveals the powerful potential of biomineralization processes.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Publisher:	American Chemical Society
ISSN:	1944-8244
Date of First Compliant Deposit:	4 December 2017
Date of Acceptance:	30 March 2017
Last Modified:	23 Nov 2024 20:15
URI:	https://orca.cardiff.ac.uk/id/eprint/107225

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