Unraveling the triplet energy transfer pathways in bacteriochlorophyll <i>b</i> -based photosynthetic complexes: insights from sub-nanosecond time-resolved absorption spectroscopy of <i>Blastochloris viridis</i>

Photosynthetic bacteria provide an excellent model for investigating the primary processes of photosynthesis due to their relatively simple photochemical systems and ease of biochemical sample preparation. While light-harvesting (LH) complexes containing bacteriochlorophyll (Bchl) a have been extensively studied, much less is known about Bchl b-based pigment-protein complexes. The purple photosynthetic bacterium Blastochloris (Blc.) viridis is unusual in possessing only an LH1-reaction center (RC) core complex. Its LH1 complex incorporates Bchl b dimers along with two distinct carotenoids-1,2-dihydroneurosporene and 1,2-dihydrolycopene. Unlike Bchl a-containing systems, this complex features a remarkably red-shifted Qy absorption band located at 1010 nm, enabling efficient LH in the near-infrared region. Beyond their role in energy transfer, carotenoids in LH1-RC complexes serve as crucial photoprotective agents, mitigating oxidative stress by quenching triplet states that could otherwise generate harmful reactive oxygen species. However, the triplet energy transfer and quenching reactions in Bchl b-containing systems remain largely unexplored. In this study, we employed sub-nanosecond time-resolved absorption spectroscopy to investigate the excitation energy transfer dynamics and photoprotective mechanisms in the purified LH1-RC and RC complexes of Blc. viridis. Our findings reveal previously uncharacterized triplet-triplet energy transfer processes from Bchl b to carotenoids. These results not only advance our understanding of Bchl b-based light-harvesting systems but also provide key insights for the development of artificial photosynthetic platforms optimized for near-infrared light utilization.