# Modulation of cyanobacterial Photosystem I protein environment and spectral capacity in response to changes in electron flow pathways and photon flux

**Authors:** Sharon L. Smolinski, Monika Tokmina-Lukaszewska, Junia M. Holland, Zhanjun Guo, Effie Kisgeropoulos, Brian Bothner, Paul W. King, Carolyn E. Lubner

PMC · DOI: 10.1016/j.jbc.2025.110233 · The Journal of Biological Chemistry · 2025-05-14

## TL;DR

This study explores how cyanobacteria adjust their photosystem I structure and function in response to changes in electron flow and light intensity.

## Contribution

The paper reveals how cyanobacterial PSI monomerization and spectral changes are linked to PsaL environment modifications.

## Key findings

- PSI monomers from ORR1 strains show altered PsaL accessibility and chlorophyll/carotenoid binding regions.
- ORR1 PSI monomers exhibit distinct spectral properties due to differences in carotenoid composition.
- Modified PSI remains functional in charge separation and electron transport despite structural changes.

## Abstract

Cyanobacterial photosystem I (PSI) can undergo modifications that adjust photosynthetic electron transport in response to fluctuations in environmental and cellular conditions. We recently reported that PSI isolated from Synechocystis sp. PCC 6803 (S. 6803) strains lacking a peripheral oxygen reduction reaction (ORR1) pathway demonstrated altered P700 photooxidation capacity, changes in spectral properties, and a higher proportion of monomers. These changes in PSI were augmented when cells were grown under higher photon flux, which creates a greater energy imbalance at PSI. We have shown that the modified PSI is functional in photochemical charge separation and ferredoxin reduction reactions. Thus, we hypothesized that monomerization of PSI was caused by changes in the environment of PsaL, which is known to be essential for stabilizing trimers. To test our hypothesis, we isolated PSI monomers and trimers from ORR1 and wild-type (WT) strains. The electron paramagnetic resonance (EPR) spectra of reduced PSI demonstrated the presence of intact FA and FB [4Fe-4S] clusters, consistent with measurements of functional charge separation and electron transport. Limited proteolysis followed by mass spectrometric analysis showed altered accessibility of PsaL in the ORRI PSI monomers compared to WT monomers, and included regions associated with chlorophyll and carotenoid binding, and in functional interactions with adjacent subunits. In addition, ORR1 PSI monomers had spectral changes compared to WT PSI due to differences in carotenoid compositions. Collectively, these findings reveal new insights into how microbes adjust PSI structure and photochemistry to mitigate photodamage in response to changes in electron utilization by downstream chemical reactions.

## Linked entities

- **Genes:** psaL (photosystem I subunit XI) [NCBI Gene 800303]
- **Proteins:** psaL (photosystem I subunit XI), LOC4338930 (ferredoxin-6, chloroplastic)
- **Chemicals:** carotenoids (PubChem CID 11227325), chlorophyll (PubChem CID 156620228)
- **Species:** Synechocystis sp. PCC 6803 (taxon 1148)

## Full-text entities

- **Chemicals:** oxygen (MESH:D010100), chlorophyll (MESH:D002734), [4Fe-4S] (-), carotenoid (MESH:D002338)
- **Species:** Synechocystis sp. (species) [taxon 1143]

## Full text

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## Figures

10 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12212252/full.md

## References

52 references — full list in the complete paper: https://tomesphere.com/paper/PMC12212252/full.md

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Source: https://tomesphere.com/paper/PMC12212252