Artificially produced [7-formyl]-chlorophyll d functions as an antenna pigment in the photosystem II isolated from the chlorophyllide a oxygenase-expressing Acaryochloris marina.

Acaryochloris marina, a chlorophyll (Chl) d-dominated cyanobacterium, is a model organism for studying photosynthesis driven by far-red light using Chl d. Furthermore, studies on A. marina may provide insights into understanding how the oxygenic photosynthetic organisms adapt after the acquisition of new Chl. To solve the reaction mechanism of its unique photosynthesis, photosystem (PS) II complexes were isolated from A. marina and analyzed. However, the lack of a molecular genetic method for A. marina prevented us from conducting further studies. We recently developed a transformation system for A. marina and we introduced a chlorophyllide a oxygenase gene into A. marina. The resultant transformant accumulated [7-formyl]-Chl d, which has never been found in nature. In the current study, we isolated PS II complexes that contained [7-formyl]-Chl d. The pigment composition of the [7-formyl]-Chl d-containing PS II complexes was 1.96±0.04 Chl a, 53.21±1.00 Chl d, and 5.48±0.33 [7-formyl]-Chl d per two pheophytin a molecules. In contrast, the composition of the control PS II complexes was 2.01±0.06 Chl a and 62.96±2.49 Chl d. The steady-state fluorescence and excitation spectra of the PS II complexes revealed that energy transfer occurred from [7-formyl]-Chl d to the major Chl d species; however, the electron transfer was not affected by the presence of [7-formyl]-Chl d. These findings demonstrate that artificially produced [7-formyl]-Chl d molecules that are incorporated into PS II replace part of the Chl d molecules and function as the antenna. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial.

Redox potential of pheophytin a in photosystem II of two cyanobacteria having the different special pair chlorophylls.

Water oxidation by photosystem (PS) II in oxygenic photosynthetic organisms is a major source of energy on the earth, leading to the production of a stable reductant. Mechanisms generating a high oxidation potential for water oxidation have been a major focus of photosynthesis research. This potential has not been estimated directly but has been measured by the redox potential of the primary electron acceptor, pheophytin (Phe) a. However, the reported values for Phe a are still controversial. Here, we measured the redox potential of Phe a under physiological conditions (pH 7.0; 25 degrees C) in two cyanobacteria with different special pair chlorophylls (Chls): Synechocystis sp. PCC 6803, whose special pair for PS II consists of Chl a, and Acaryochloris marina MBIC 11017, whose special pair for PS II consists of Chl d. We obtained redox potentials of -536 +/- 8 mV for Synechocystis sp. PCC 6803 and -478 +/- 24 mV for A. marina on PS II complexes in the presence of 1.0 M betaine. The difference in the redox potential of Phe a between the two species closely corresponded with the difference in the light energy absorbed by Chl a versus Chl d. We estimated the potentials of the special pair of PS II to be 1.20 V and 1.18 V for Synechocystis sp. PCC 6803 (P680) and A. marina (P713), respectively. This clearly indicates conservation in the properties of water-oxidation systems in oxygenic photosynthetic organisms, irrespective of the special-pair chlorophylls.