PROBING ELECTRON TRANSFER OF THE REDOX SPECIES IN WILD-TYPE RC PROTEIN AND ITS PIGMENT-REPLACED MUTANTS RE-CONSTITUTED IN SELF-ASSEMBLY MONOLAYERS

Abstract

The multi-layered protein film, containing photosynthetic reaction center (RC) protein isolated from Rhodobacter sphaeriodes or its pigment-replaced mutants, was prepared with 4-Aminothiophenol (4-ATP) self-assembled monolayer (SAM) modified gold electrode. The RC protein was embedded in an ordered-orientated charged poly-styrenesulfonate (PSS) and poly(dimerthyldiallylammonium) chloride (PDDA) film successively. The reversible or quasi-reversible electron transfer (ET) for the re-constituted RC and its mutants was probed by cyclic voltammetry (CV) and square wave voltammetry (SWV), reflecting the electrochemical-driven electron recombination for RC protein or its mutants. The SWV data for RC and its mutants in the films were non-linearly fitted to get the electrochemical parameters.

Keywords:

• Photosynthetic reaction center
• Rhodobacter sphaeroides
• Self-assembly monolayer

ACKNOWLEDGMENT

This work is supported by NSFC projects No. 39970195, 29905001, 39730040 & G1998010100.