Dataset Information

Photosystem II assembly No-reaction center (NRC) complex

ABSTRACT: LC-MS/MS identification of small subunit peptides of Photosystem II assembly intermediate (NRC) with/without trypsin digestion. Peptide sequence identification with HCD fragmentation using Q-Exactive plus mass spectrometer (Thermo-Fisher)

INSTRUMENT(S): Q Exactive

ORGANISM(S): Synechocystis Sp. Pcc 6803

TISSUE(S): Photosynthetic Cell, Cell Culture

SUBMITTER: Haijun Liu

LAB HEAD: Himadri B Pakrasi

PROVIDER: PXD013406 | Pride | 2019-10-14

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20190405_NRC_47.raw_Haijun_Liu.mgf	Mgf
	20190405_NRC_47.raw_Haijun_Liu.mzid.gz	Mzid
	20190405_NRC_47.raw_Haijun_Liu.pride.mgf.gz	Mgf
	20190405_NRC_47.raw_Haijun_Liu.pride.mztab.gz	Mztab
	20190405_NRC_dO.raw_Haijun_Liu.mgf	Mgf

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Publications

A novel chlorophyll protein complex in the repair cycle of photosystem II.

Weisz Daniel A DA Johnson Virginia M VM Niedzwiedzki Dariusz M DM Shinn Min Kyung MK Liu Haijun H Klitzke Clécio F CF Gross Michael L ML Blankenship Robert E RE Lohman Timothy M TM Pakrasi Himadri B HB

Proceedings of the National Academy of Sciences of the United States of America 20191008 43

In oxygenic photosynthetic organisms, photosystem II (PSII) is a unique membrane protein complex that catalyzes light-driven oxidation of water. PSII undergoes frequent damage due to its demanding photochemistry. It must undergo a repair and reassembly process following photodamage, many facets of which remain unknown. We have discovered a PSII subcomplex that lacks 5 key PSII core reaction center polypeptides: D1, D2, PsbE, PsbF, and PsbI. This pigment-protein complex does contain the PSII core ...[more]

PMID: 31594847

Similar Datasets

Project description:Photosystem II (PSII) is a multisubunit pigment-protein complex that uses light-induced charge separation to power oxygenic photosynthesis. Its reaction center chromophores, where the charge transfer cascade is initiated, are arranged symmetrically along the D1 and D2 core polypeptides and comprise four chlorophyll (PD1, PD2, ChlD1, ChlD2) and two pheophytin molecules (PheoD1 and PheoD2). Evolution favored productive electron transfer only via the D1 branch, with the precise nature of primary excitation and the factors that control asymmetric charge transfer remaining under investigation. Here we present a detailed atomistic description for both. We combine large-scale simulations of membrane-embedded PSII with high-level quantum-mechanics/molecular-mechanics (QM/MM) calculations of individual and coupled reaction center chromophores to describe reaction center excited states. We employ both range-separated time-dependent density functional theory and the recently developed domain based local pair natural orbital (DLPNO) implementation of the similarity transformed equation of motion coupled cluster theory with single and double excitations (STEOM-CCSD), the first coupled cluster QM/MM calculations of the reaction center. We find that the protein matrix is exclusively responsible for both transverse (chlorophylls versus pheophytins) and lateral (D1 versus D2 branch) excitation asymmetry, making ChlD1 the chromophore with the lowest site energy. Multipigment calculations show that the protein matrix renders the ChlD1 → PheoD1 charge-transfer the lowest energy excitation globally within the reaction center, lower than any pigment-centered local excitation. Remarkably, no low-energy charge transfer states are located within the "special pair" PD1-PD2, which is therefore excluded as the site of initial charge separation in PSII. Finally, molecular dynamics simulations suggest that modulation of the electrostatic environment due to protein conformational flexibility enables direct excitation of low-lying charge transfer states by far-red light.