Structural basis for energy and electron transfer of the photosystem I–IsiA–flavodoxin supercomplex

Cao, Peng; Cao, Duanfang; Long, Si; Su, Xiaodong; Tian, Lijin; Chang, Wenrui; Liu, Zhongfan; Zhang, Xinzheng; Li, Mei

doi:10.1038/s41477-020-0593-7

Cited by 57 publications

(71 citation statements)

References 63 publications

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“…The first closed IsiA ring associated with PSI commonly consists of 18 peaks of IsiA monomers ( Fig. 4a), consistent with the EM results 6,7,11,12,15 (Fig. 1h).…”

Section: Distribution and Structural Heterogeneity Of Isia−psi Supercsupporting

confidence: 88%

“…3a). Contrary to the homogeneous structure obtained from averaged EM images 6,7,11,12,15,31 , AFM images revealed the inherent structural variability of IsiA−PSI supercomplexes in native thylakoid membranes ( Fig. 3b-3f, Supplementary Figs.…”

Section: Distribution and Structural Heterogeneity Of Isia−psi Supercmentioning

confidence: 65%

“…1g), resembling the IsiA−PSI complexes from ironlimited cyanobacteria (Fig. 1h) 6,7,11,12 . The overall height of IsiA proteins is 4.3 ± 0.1 nm (n = 5), less than that of PSI without PsaC, PsaD, and PsaE (5.0 ± 0.1 nm, n = 15) ( Supplementary Fig.…”

Section: High Light Induces Isia Expression and Formation Of The Isiamentioning

confidence: 82%

“…It has been proposed to function as an accessory antenna for PSI. Recent electron microscopy revealed that each IsiA monomer coordinates 17 chlorophyll (Chl) molecules and 18 IsiA can encircle a PSI trimer to form an IsiA−PSI supercomplex 11,12 .…”

Section: Introductionmentioning

confidence: 99%

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Structural variability, coordination and adaptation of a native photosynthetic machinery

et al. 2020

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Cyanobacterial thylakoid membranes represent the active sites for both photosynthetic and respiratory electron transport. We used high-resolution atomic force microscopy to visualise the native organisation and interactions of photosynthetic complexes within the thylakoid membranes from the model cyanobacterium Synechococcus elongatus PCC 7942. The thylakoid membranes are heterogeneous and assemble photosynthetic complexes into functional domains to enhance their coordination and regulation. Under high light, the chlorophyll-binding proteins IsiA are strongly expressed and associates with Photosystem I (PSI) forming highly variable IsiA−PSI supercomplexes to increase the absorption cross-section of PSI. There are also tight interactions of PSI with Photosystem II (PSII), cytochrome b 6 f, ATP synthase, and NAD(P)H dehydrogenase complexes. The organisational variability of these photosynthetic supercomplexes permits efficient linear and cyclic electron transport and bioenergetic regulation. Understanding the organisational landscape and environmental adaptation of cyanobacterial thylakoid membranes may help inform strategies for engineering efficient photosynthetic systems and photo-biofactories.

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“…The first closed IsiA ring associated with PSI commonly consists of 18 peaks of IsiA monomers ( Fig. 4a), consistent with the EM results 6,7,11,12,15 (Fig. 1h).…”

Section: Distribution and Structural Heterogeneity Of Isia−psi Supercsupporting

confidence: 88%

Section: Distribution and Structural Heterogeneity Of Isia−psi Supercmentioning

confidence: 65%

Section: High Light Induces Isia Expression and Formation Of The Isiamentioning

confidence: 82%

Section: Introductionmentioning

confidence: 99%

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Structural variability, coordination and adaptation of a native photosynthetic machinery

et al. 2020

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“…The short loop present in Synechocystis can be found in Synechococcus sp. PCC 7942 49 and Chroococcidiopsis sp. TS-821 ( PDBID: 6QWJ ) 50 .…”

Section: Discussionmentioning

confidence: 99%

The structure of a red-shifted photosystem I reveals a red site in the core antenna

et al. 2020

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Photosystem I coordinates more than 90 chlorophylls in its core antenna while achieving near perfect quantum efficiency. Low energy chlorophylls (also known as red chlorophylls) residing in the antenna are important for energy transfer dynamics and yield, however, their precise location remained elusive. Here, we construct a chimeric Photosystem I complex in Synechocystis PCC 6803 that shows enhanced absorption in the red spectral region. We combine Cryo-EM and spectroscopy to determine the structure−function relationship in this red-shifted Photosystem I complex. Determining the structure of this complex reveals the precise architecture of the low energy site as well as large scale structural heterogeneity which is probably universal to all trimeric Photosystem I complexes. Identifying the structural elements that constitute red sites can expand the absorption spectrum of oxygenic photosynthetic and potentially modulate light harvesting efficiency.

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Structure, Organization and Function of Light-Harvesting Complexes Associated with Photosystem II

Wang

Shen

2021

Advances in Photosynthesis and Respiration

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Structural basis for energy and electron transfer of the photosystem I–IsiA–flavodoxin supercomplex

Cited by 57 publications

References 63 publications

Structural variability, coordination and adaptation of a native photosynthetic machinery

Structural variability, coordination and adaptation of a native photosynthetic machinery

The structure of a red-shifted photosystem I reveals a red site in the core antenna

Structure, Organization and Function of Light-Harvesting Complexes Associated with Photosystem II

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