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

Bioengineered. 2012 Sep-Oct;3(5):275-9. doi: 10.4161/bioe.21048. Epub 2012 Sep 1.

Abstract

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.

MeSH terms

  • Aspartic Acid / chemistry
  • Aspartic Acid / genetics
  • Bacteriorhodopsins / chemistry*
  • Bacteriorhodopsins / genetics
  • Bacteriorhodopsins / metabolism
  • Electrochemical Techniques
  • Escherichia coli / genetics
  • Genetic Engineering / methods*
  • Glycine max / chemistry
  • Ion Transport
  • Kinetics
  • Light
  • Mutagenesis, Site-Directed
  • Mutation*
  • Nanoparticles / chemistry
  • Photochemical Processes
  • Protons*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Serine / chemistry
  • Serine / genetics
  • Spectrum Analysis
  • Valine / chemistry
  • Valine / genetics

Substances

  • Protons
  • Recombinant Proteins
  • Aspartic Acid
  • Serine
  • Bacteriorhodopsins
  • Valine