Results 111 to 120 of about 1,718 (152)

Three rate-determining protein roles in photosynthetic O₂-evolution addressed by time-resolved experiments on genetically modified photosystems. [PDF]

Nat Commun
Mäusle SM, Parisse G, Assunção R, De Santis C, Simon PS, Narzi D, Guidoni L, Debus RJ, Dau H.   +8 more
europepmc   +1 more source

Mutation-induced shift of the photosystem II active site reveals insight into conserved water channels. [PDF]

J Biol Chem
Flesher DA, Liu J, Wang J, Gisriel CJ, Yang KR, Batista VS, Debus RJ, Brudvig GW.   +7 more
europepmc   +1 more source

Structure of a unique PSII-Pcb tetrameric megacomplex in a chlorophyll <i>d</i>-containing cyanobacterium. [PDF]

Sci Adv
Shen L, Gao Y, Tang K, Qi R, Fu L, Chen JH, Wang W, Ma X, Li P, Chen M, Kuang T, Zhang X, Shen JR, Wang P, Han G.   +14 more
europepmc   +1 more source

Photosystem II supercomplexes lacking light-harvesting antenna protein LHCB5 and their organization in the thylakoid membrane. [PDF]

Physiol Plant
Vánská T, Kouřil R, Opatíková M, Ilíková I, Arshad R, Roudnický P, Ilík P.   +6 more
europepmc   +1 more source

Thylakoid protein FPB1 synergistically cooperates with PAM68 to promote CP47 biogenesis and Photosystem II assembly. [PDF]

Nat Commun
Zhang L, Ruan J, Gao F, Xin Q, Che LP, Cai L, Liu Z, Kong M, Rochaix JD, Mi H, Peng L.   +10 more
europepmc   +1 more source

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Energy dissipation efficiency in the CP43 assembly intermediate complex of photosystem II

Biochimica Et Biophysica Acta - Bioenergetics, 2023
Photosystem II in oxygenic organisms is a large membrane bound rapidly turning over pigment protein complex. During its biogenesis, multiple assembly intermediates are formed, including the CP43-preassembly complex (pCP43). To understand the energy transfer dynamics in pCP43, we first engineered a His-tagged version of the CP43 in a CP47-less strain of
Himadri Pakrasi, Niedźwiedzki Dariusz, Sandeep Biswas   +2 more
exaly   +3 more sources

Spectral properties of the CP43-deletion mutant of Synechocystis sp. PCC 6803

Photosynthesis Research, 2008
Spectral properties, particularly fluorescence spectra and their time-dependent behavior, were investigated for a mutant of the cyanobacterium Synechocystis sp. PCC 6803 lacking the 43 kDa chlorophyll-protein (CP43, PsbC). Lack of CP43 was confirmed by a size shift of the corresponding gene and by Western blotting.
Seiji Akimoto, Tatsuya Tomo, Yuichiro Shimada   +2 more
exaly   +3 more sources

Heat-induced unfolding of apo-CP43 studied by fluorescence spectroscopy and CD spectroscopy

Photosynthesis Research, 2015
CP43 is a chlorophyll-binding protein, which acts as a conduit for the excitation energy transfer. The thermal stability of apo-CP43 was studied by intrinsic fluorescence, exogenous ANS fluorescence, and circular dichroism spectroscopy. Under heat treatment, the structure of apo-CP43 changed and existed transition state occurred between 56 and 62 °C by
Lin-Fang Du
exaly   +3 more sources

Crystallisation of CP43, a Chlorophyll Binding Protein of Photosystem II: An Electron Microscopy Analysis of Molecular Packing

Journal of Structural Biology, 2000
Microcrystals of the chlorophyll binding protein, CP43, isolated from spinach thylakoid membranes have been studied by electron microscopy both in negative stain and in vitreous ice. Image analyses of three characteristic views show that the crystals are built of five different layers perpendicular to the c-axis.
Claudia Büchel, Edward Morris, James Barber   +2 more
exaly   +3 more sources

The structure and function of CP47 and CP43 in Photosystem II

Photosynthesis Research, 2002
This Minireview presents a summary of recent investigations examining the structure and functions of the Photosystem II chlorophyll-proteins CP47 and CP43, updating our previous review which appeared in 1990 (TM Bricker, Photosynth Res 24: 1-13).
Terry M, Bricker, Laurie K, Frankel
openaire   +2 more sources