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ProteomicsAPX2, the ascorbate peroxidase-related protein, regulates the levels of plastocyanin in Chlamydomonas
The function of ascorbate peroxidase-related (APX-R) proteins, present in all green photosynthetic eukaryotes, remains unclear. This study focuses on APX-R from Chlamydomonas reinhardtii, namely ascorbate peroxidase 2 (APX2). We showed that apx2 mutants exhibited a faster oxidation of the PSI primar...
ORGANISM(S): Chlamydomonas reinhardtii 
2024-01-29 | PXD046605 | Pride
Chlamydomonas Apx2 Plastocyanin Cytochrome c6 Copper-deficiency P700 
ProteomicsChemical crosslinking of plastocyanin and the cytochrome b6f complex
In this work we investigated the role of plastocyanin (PC) phosphorylation in photosynthetic electron transfer, focusing on PC's interaction with both cytochrome b6f, (Cytb6f) and photosystem I (PSI) in Chlamydomonas reinhardtii. While the binding and electron transfer between PC and PSI are well ch...
ORGANISM(S): Chlamydomonas reinhardtii 
2025-08-25 | PXD060078 | Pride
Cytochrome b6f Plastocyanin Chlamzdomonas Edc Crosslinking 
UnknownAPX2 Is an Ascorbate Peroxidase-Related Protein that Regulates the Levels of Plastocyanin in Chlamydomonas.
Not available
S-EPMC11094752 | biostudies-literature
UnknownInsights into plastocyanin-cytochrome b6f complex formation: The role of plastocyanin phosphorylation.
Not available
S-EPMC12341890 | biostudies-literature
UnknownAscorbate Peroxidase 2 (APX2) of Chlamydomonas Binds Copper and Modulates the Copper Insertion into Plastocyanin.
Not available
S-EPMC10669542 | biostudies-literature
UnknownModeling Diffusive Motion of Ferredoxin and Plastocyanin on the PSI Domain of <i>Procholorococcus marinus</i> MIT9313.
Not available
S-EPMC12060261 | biostudies-literature
UnknownPlastocyanin and Cytochrome f Complex Structures Obtained by NMR, Molecular Dynamics, and AlphaFold 3 Methods Compared to Cryo-EM Data.
Not available
S-EPMC11507376 | biostudies-literature
UnknownA QM/MM study of the nature of the entatic state in plastocyanin.
Not available
S-EPMC5434870 | biostudies-literature
ProteomicsAbsolute quantification of selected photosynthetic electron transfer proteins in Chlamydomonas reinhardtii in the presence and absence of oxygen
The absolute amount of plastocyanin (PC), ferredoxin-NADP+-oxidoreductase (FNR), hydrogenase (HYDA1) and ferredoxin 5 (FDX5) were quantified in aerobic and anaerobic Chlamydomonas reinhardtii whole cells using purified (recombinant) proteins as internal standard in a mass spectrometric approach. Qua...
ORGANISM(S): Chlamydomonas reinhardtii 
2022-02-23 | PXD008313 | Pride
Ferredoxin-nadp+-oxidoreductase Plastocyanin Ferredoxin 5 Hydrogenase Absolute quantification Chlamydomonas reinhardtii 
UnknownStructure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions.
Not available
S-EPMC8238519 | biostudies-literature
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