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Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties

Dunleavy, Robert, Lu, Li, Kiely, Christopher J., McIntosh, Steven and Berger, Bryan W. 2016. Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties. Proceedings of the National Academy of Sciences 113 (19) , pp. 5275-5280. 10.1073/pnas.1523633113

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Abstract

Nature has evolved several unique biomineralization strategies to direct the synthesis and growth of inorganic materials. These natural systems are complex, involving the interaction of multiple biomolecules to catalyze biomineralization and template growth. Herein we describe the first report to our knowledge of a single enzyme capable of both catalyzing mineralization in otherwise unreactive solution and of templating nanocrystal growth. A recombinant putative cystathionine γ-lyase (smCSE) mineralizes CdS from an aqueous cadmium acetate solution via reactive H2S generation from l-cysteine and controls nanocrystal growth within the quantum confined size range. The role of enzymatic nanocrystal templating is demonstrated by substituting reactive Na2S as the sulfur source. Whereas bulk CdS is formed in the absence of the enzyme or other capping agents, nanocrystal formation is observed when smCSE is present to control the growth. This dual-function, single-enzyme, aerobic, and aqueous route to functional material synthesis demonstrates the powerful potential of engineered functional material biomineralization.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Cardiff Catalysis Institute (CCI)
Publisher: National Academy of Sciences
ISSN: 0027-8424
Date of First Compliant Deposit: 3 October 2017
Date of Acceptance: 4 April 2016
Last Modified: 11 Mar 2020 19:26
URI: http://orca-mwe.cf.ac.uk/id/eprint/105153

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