Primary light-energy conversion in tetrameric chlorophyll structure of photosystemII and bacterial reaction centers: I. A review

The purpose of the review is to show that the tetrameric (bacterio)chlorophyll ((B)Chl) structures in reaction centers of photosystem II (PSII) of green plants and in bacterial reaction centers (BRCs) are similar and play a key role in the primary charge separation. The Stark effect measurements on PSII reaction centers have revealed an increased dipole moment for the transition at ~730nm (Frese etal., Biochemistry 42:9205-9213, 2003). It was found (Heber and Shuvalov, Photosynth Res 84:84-91, 2005) that two fluorescent bands at 685 and 720nm are observed in different organisms. These two forms are registered in the action spectrum of Q sub(A) photoreduction. Similar results were obtained in core complexes of PSII at low temperature (Hughes etal., Biochim Biophys Acta 1757: 841-851, 2006). In all cases the far-red absorption and emission can be interpreted as indication of the state with charge transfer character in which the chlorophyll monomer plays a role of an electron donor. The role of bacteriochlorophyll monomers (B sub(A) and B sub(B)) in BRCs can be revealed by different mutations of axial ligand for Mg central atoms. RCs with substitution of histidine L153 by tyrosine or leucine and of histidine M182 by leucine (double mutant) are not stable in isolated state. They were studied in antennaless membrane by different kinds of spectroscopy including one with femtosecond time resolution. It was found that the single mutation (L153HY) was accompanied by disappearance of B sub(A) molecule absorption near 802nm and by 14-fold decrease of photochemical activity measured with ms time resolution. The lifetime of P sub(870)* increased up to ~200ps in agreement with very low rate of the electron transfer to A-branch. In the double mutant L153HY+M182HL, the B sub(A) appears to be lost and B sub(B) is replaced by bacteriopheophytin sub(B) with the absence of any absorption near 800nm. Femtosecond measurements have revealed the electron transfer to B-branch with a time constant of ~2ps. These results are discussed in terms of obligatory role of B sub(A) and sub(B) molecules located near P for efficient electron transfer from P*.