We have generated a novel model protein for an artificial light-harvesting complex composed of two proteins, cytochrome b562 (cytb562) and enhanced green fluorescent protein (EGFP), in which two chromophores are fixed in each protein matrix. Cytb562 was appended to the N-terminus of EGFP via a Gly-Ser linker and the resultant fusion protein was successfully expressed in Escherichia coli as a mixture of the apo- and the holo-forms as to the cytb562 moiety. The fluorescence of EGFP was substantially quenched when the apo-form was reconstituted with hemin. Based on the fluorescence lifetime measurements, it appeared that light energy entrapped by EGFP is transferred to the heme of cytb562 by resonance energy transfer (energy transfer yield: 65%). Spatial organization of two chromophores using small and stable protein matrices will be promising toward the construction of an artificial light-harvesting complex by protein engineering.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - Nov 23 2001|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology