Results 1 to 10 of about 20,925 (163)
Cryo-EM structure of Chlamydomonas reinhardtii Photosystem I complexed with cytochrome c 6 [PDF]
Photosynthetic electron transfer relies on small soluble carriers that shuttle electrons between the cytochrome b₆f complex and Photosystem I (PSI). While copper-containing plastocyanin (Pc) serves this role in plants, the heme protein cytochrome c₆ (Cyt
Yu Ogawa +6 more
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An efficient clear-native PAGE–based workflow for cryo-electron microscopy sample preparation of large protein complexes [PDF]
Background Cryo-electron microscopy (cryo-EM) has revolutionized protein research by enabling high-resolution structural analysis. However, preparing ultra-large protein complexes (e.g., > 700 kDa) for cryo-EM remains challenging, as it requires ...
Zitong Yang +6 more
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Light absorbed by chlorophylls of Photosystems II and I drives oxygenic photosynthesis. Light-harvesting complexes increase the absorption cross-section of these photosystems.
Hamed Sattari Vayghan +10 more
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Chlorophyll‐protein complexes of barley photosystem I [PDF]
Photosystem I (PSI) preparations with a chlorophyll a/b ratio of 6.0 were isolated from barley thylakoids using two different methods. The high‐molecular‐mass complex (CP1a*) which is resolved by non‐denaturing gel electrophoresis had the same properties as a PSI preparation (PSI‐200) isolated by Triton X‐100 solubilisation of thylakoids followed by ...
R, Bassi, D, Simpson
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The unicellular green alga, Chlamydomonas reinhardtii, has been widely used as a model system to study photosynthesis. Its possibility to generate and analyze specific mutants has made it an excellent tool for mechanistic and biogenesis studies.
Tom Schwartz +3 more
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Evidence for a chlorophylla/b—protein complex associated with Photosystem II [PDF]
A new chlorophylla/b—protein complex designated as LHCPx was separated by SDS—PAGE. This complex differs from the light‐harvesting chla/b—protein of PS II, by its chla/bratio, its fluorescence properties and its apoprotein composition. Evidence is provided that this complex corresponds to a part of PS I antenna.
Remy, R., Ambard-Bretteville, F.
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The Assembly of Super-Complexes in the Plant Chloroplast
Increasing evidence has revealed that the enzymes of several biological pathways assemble into larger supramolecular structures called super-complexes. Indeed, those such as association of the mitochondrial respiratory chain complexes play an essential ...
Kezhen Qin +2 more
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Crystallization of the Large Membrane Protein Complex Photosystem I in a Microfluidic Channel [PDF]
Traditional macroscale protein crystallization is accomplished nontrivially by exploring a range of protein concentrations and buffers in solution until a suitable combination is attained. This methodology is time-consuming and resource-intensive, hindering protein structure determination.
Bahige G, Abdallah +3 more
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Properties of photosystem I antenna protein complexes of the diatom Cyclotella meneghiniana [PDF]
Analysis of photosystem I (PSI) complexes from Cyclotella meneghiniana cultured under different growth conditions led to the identification of three groups of antenna proteins, having molecular weights of around 19, 18, and 17 kDa. The 19-kDa proteins have earlier been demonstrated to be more peripherally bound to PSI, and their amount in the PSI ...
Juhas, Matthias, Büchel, Claudia
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Self-assembling peptide detergents stabilize isolated photosystem I on a dry surface for an extended time. [PDF]
We used a class of designed peptide detergents to stabilize photosystem I (PS-I) upon extended drying under N2 on a gold-coated-Ni-NTA glass surface. PS-I is a chlorophyll-containing membrane protein complex that is the primary reducer of ferredoxin and ...
Patrick Kiley +5 more
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