Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 174, Issue -, Pages 42-51Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.01.141
Keywords
Biosynthesis; Quantum dots; Structural biology
Funding
- National Natural Science Foundation of China [31770801]
- Natural Science Foundation of Guangdong Province [2018B030306029, 2017A030313145]
- Sun Yat-Sen University
Ask authors/readers for more resources
The study identified a novel bacterial biomolecule that drives the synthesis of nanomaterials, with the mechanism of synthesis still unclear. Structural changes and the specificity of surface amino acids within the active sites were found to be crucial for the protein-driven synthesis of metal sulfide quantum dots, allowing for control over the size and morphology of the synthesized products through protein modification.
The development and utilization of inorganic material biosynthesis have evolved into single macromolecular systems. A putative cystathionine gamma-lyase of bacteria .Stenotrophomonas maltophilia (smCSE) is a newly identified biomolecule that enables the synthesis of nanomaterials. Due to the lack of structural information, the mechanism of smCSE biosynthesis remains unclear. Herein, we obtain two atomic-resolution smCSE-form X-ray structures and confirm that the conformational changes of Tyr108 and Lys206 within the enzyme active sites are critical for the protein-driven synthesis of metal sulfide quantum dots (QDs). The structural stability of tetramer and the specificity of surface amino acids are the basis for smCSE to synthesize quantum dots. The size of QD products can be regulated by predesigned amino acids and the morphology can be controlled through proteolytic treatments. The growth rate is enhanced by the stabilization of a flexible loop in the active site, as shown by the X-ray structure of the engineered protein which fused with a dodecapeptide. We further prove that the smCSE-driven route can be applied to the general synthesis of other metal sulfide nanoparticles. These results provide a better understanding of the mechanism of QD biosynthesis and a new perspective on the control of this biosynthesis by protein modification. (C) 2021 Published by Elsevier B.V.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available