Generation and analysis of bacteriorhodopsin mutants with the potential for biotechnological applications

The properties of bacteriorhodopsin (BR) can be manipulated by genetic engineering. Therefore, by the methods of gene engineering, Asp85 was replaced individually by two other amino acids (D85V, D85S). The resulting recombinant proteins were assembled into soybean vesicles retinylated to form functi...

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Bibliographic Details
Published in:Bioengineered 2012-09, Vol.3 (5), p.275-279
Main Authors: Saeedi, P., Moosaabadi, J. Mohammadian, Sebtahmadi, S. Sina, Mehrabadi, J. Fallah, Behmanesh, M., Nejad, H. Rouhani, Nazaktabar, A.
Format: Article
Language:English
Subjects:
Absorption spectra
Aspartic Acid - chemistry
Aspartic Acid - genetics
Bacteriorhodopsin
Bacteriorhodopsins - chemistry
Bacteriorhodopsins - genetics
Bacteriorhodopsins - metabolism
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Electrochemical Techniques
Escherichia coli - genetics
Genetic Engineering - methods
Glycine max - chemistry
Ion Transport
Kinetics
Landes
Light
Mutagenesis, Site-Directed
Mutants
Mutation
Nanoparticles - chemistry
Organogenesis
Photochemical Processes
Proteins
Proton pumping
Protons
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Research Paper
Serine - chemistry
Serine - genetics
Site-directed mutagenesis
Spectrum Analysis
Valine - chemistry
Valine - genetics
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Summary:The properties of bacteriorhodopsin (BR) can be manipulated by genetic engineering. Therefore, by the methods of gene engineering, Asp85 was replaced individually by two other amino acids (D85V, D85S). The resulting recombinant proteins were assembled into soybean vesicles retinylated to form functional BR-like nano-particles. Proton translocation was almost completely abrogated by the mutant D85S, while the D85V mutant was partially active in pumping protons. Compared with wild type, maximum absorption of the mutants, D85V and D85S, were 563 and 609 nm, which illustrated 5 nm reductions (blue shift) and 41 nm increases (red shift), respectively. Since proton transport activity and spectroscopic activities of the mutants are different, a wide variety of membrane bioreactors (MBr) have been developed. Modified proteins can be utilized to produce unique photo/Electro-chromic materials and tools.
ISSN:2165-5979
2165-5987
DOI:10.4161/bioe.21048