Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light

Gisriel, Christopher J.; Shen, Gaozhong; Flesher, David A.; Kurashov, Vasily; Golbeck, John H.; Brudvig, Gary W.; Amin, Muhamed; Bryant, Donald A.

doi:10.1016/j.jbc.2022.102815

Cited by 22 publications

(41 citation statements)

References 72 publications

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“…These residues occur in the vicinity of a bound ß‐carotene (Car D1 ) and the accessory chlorophyll, ChlZ D1 , and may alter the position of the ß‐carotene (Nürnberg et al, 2018). In the FRL‐PS II centres, the ChlZ D1 is a chlorophyll a molecule (Gisriel et al, 2023). This chlorophyll has been indicated to be responsible for energy transfer from CP43 to the reaction centre (Yang et al, 2022).…”

Section: Resultsmentioning

confidence: 99%

“…The Phe119 residue is within 5 Å of the C2 position of ring 1 of Chl D1 , which is a chlorophyll d molecule in FRL-PS II centres (Gisriel et al, 2023;Nürnberg et al, 2018).…”

Section: Introduction Of Characteristic Mutations Associated With D1 ...mentioning

confidence: 99%

“…Typically, a FaRLiP gene cluster encodes modified versions of the core PS II proteins: CP43, CP47, D2, and two versions of D1 as well as PsbH and usually includes the genes encoding the PS I proteins, PsaA/B/F/I/J/L, and the phycobiliproteins: ApcA/B/D/E (Gan et al, 2015; Sheridan et al, 2020). In addition, some of the chlorophyll a molecules in PS I and PS II are replaced by chlorophyll d and chlorophyll f , resulting in absorption of light at wavelengths longer than 700 nm (Gisriel et al, 2022b; 2023; Nürnberg et al, 2018; Shen et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…Modified FRL‐PS II contains four chlorophyll f molecules and one chlorophyll d molecule. The chlorophyll d molecule replaces the P 680 Chl D1 chlorophyll a (Figure 1; Gisriel et al, 2023). One chlorophyll f is associated with CP43 and the remaining three are associated with CP47 (Figure 1; Gisriel et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

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Expression of the far‐red D1 protein or introduction of conserved far‐red D1 residues into Synechocystis sp. PCC 6803 impairs Photosystem II

Sheridan,

Brown,

Eaton‐Rye

et al. 2023

Physiologia Plantarum

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The wavelengths of light harvested in oxygenic photosynthesis are ~400–700 nm. Some cyanobacteria respond to far‐red light exposure via a process called far‐red light photoacclimation which enables absorption of light at wavelengths >700 nm and its use to support photosynthesis. Far‐red‐light‐induced changes include up‐regulation of alternative copies of multiple proteins of Photosystem II (PS II). This includes an alternative copy of the D1 protein, D1FR. Here, we show that D1FR introduced into Synechocystis sp. PCC 6803 (hereafter Synechocystis 6803) can be incorporated into PS II centres that evolve oxygen at low rates but cannot support photoautotrophic growth. Using mutagenesis to modify the psbA2 gene of Synechocystis 6803, we modified residues in helices A, B, and C to be characteristic of D1FR residues. Modification of the Synechocystis 6803 helix A to resemble the D1FR helix A, with modifications in the region of the bound ß‐carotene (CarD1) and the accessory chlorophyll, ChlZD1, produced a strain with a similar phenotype to the D1FR strain. In contrast, the D1FR changes in helices B and C had minor impacts on photoautotrophy but impacted the function of PS II, possibly through a change in the equilibrium for electron sharing between the primary and secondary plastoquinone electron acceptors QA and QB in favour of QA−. The addition of combinations of residue changes in helix C indicates compensating effects may occur and highlight the need to experimentally determine the impact of multiple residue changes.

show abstract

Section: Resultsmentioning

confidence: 99%

“…The Phe119 residue is within 5 Å of the C2 position of ring 1 of Chl D1 , which is a chlorophyll d molecule in FRL-PS II centres (Gisriel et al, 2023;Nürnberg et al, 2018).…”

Section: Introduction Of Characteristic Mutations Associated With D1 ...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Expression of the far‐red D1 protein or introduction of conserved far‐red D1 residues into Synechocystis sp. PCC 6803 impairs Photosystem II

Sheridan,

Brown,

Eaton‐Rye

et al. 2023

Physiologia Plantarum

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show abstract

“…The formyl group of Chl b -606 is hydrogen bonded to the water molecule, which is an axial ligand of Chl b -607. These interactions were assessed via a python-based tool that searches for potential H-bond donor partnering to the formyl groups of any set of Chl-containing atomic coordinates to help predict the Chl type selectivity . MCCE identifies these five Chl sites with hydrogen bonds but misses Chl 601.…”

Section: Discussionmentioning

confidence: 99%

Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II

Ranepura,

Mao,

Vermaas

et al. 2023

J. Phys. Chem. B

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A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center

Gisriel,

Flesher,

Long

et al. 2023

Photosynth Res

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Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light

Cited by 22 publications

References 72 publications

Expression of the far‐red D1 protein or introduction of conserved far‐red D1 residues into Synechocystis sp. PCC 6803 impairs Photosystem II

Expression of the far‐red D1 protein or introduction of conserved far‐red D1 residues into Synechocystis sp. PCC 6803 impairs Photosystem II

Computing the Relative Affinity of Chlorophylls a and b to Light-Harvesting Complex II

A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center

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