期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 19, 页码 5275-5280出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1523633113
关键词
cadmium sulfide; quantum dot; biomineralization; enzyme; nanoparticle
资金
- National Science Foundation under Emerging Frontiers in Research and Innovation-Photosynthetic Bioreactor (EFRI-PSBR) Program [1332349]
- Lehigh University Collaborative Research Opportunity program
- Directorate For Engineering
- Emerging Frontiers & Multidisciplinary Activities [1332349] Funding Source: National Science Foundation
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 gamma-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 dualfunction, single-enzyme, aerobic, and aqueous route to functional material synthesis demonstrates the powerful potential of engineered functional material biomineralization.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据