[NMR paper] An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Related ArticlesAn NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Biochim Biophys Acta. 2013 Mar 4;
Authors: Pandit A, Reus M, Morosinotto T, Bassi R, Holzwarth AR, de Groot HJ
Abstract
To protect the photosynthetic apparatus against photo-damage in high sunlight, the photosynthetic antenna of oxygenic organisms can switch from a light-harvesting to a photoprotective mode through the process of Non-Photochemical Quenching (NPQ). There is growing evidence that light-harvesting proteins of photosystem II participate in photoprotection by a built-in capacity to switch their conformation between light-harvesting and energy-dissipating states. Here we applied high-resolution Magic-Angle Spinning NMR on uniformly 13C-enriched major light-harvesting complex II (LHCII) of Chlamydomonas reinhardtii in active or quenched states. Our results reveal that the switch into a dissipative state is accompanied by subtle changes in the chlorophyll (Chl) a ground-state electronic structures that affect their NMR responses, particularly for the macrocycle 13C4, 13C5 and 13C6 carbon atoms. Inspection of the LHCII X-ray structures shows that of the Chl molecules in the terminal emitter domain, where excited-state energy accumulates prior to further transfer or dissipation, the C4, 5 and 6 atoms are in closest proximity to lutein; supporting quenching mechanisms that involve altered Chl-lutein interactions in the dissipative state. In addition the observed changes could represent altered interactions between Chla and neoxanthin, which alters its configuration under NPQ conditions. The Chls appear to have increased dynamics in unquenched, detergent-solubilized LHCII. Our work demonstrates that solid-state NMR is applicable to investigate high-resolution structural details of light-harvesting proteins in varied functional conditions, and represents a valuable tool to address their molecular plasticity associated with photoprotection.
PMID: 23466337 [PubMed - as supplied by publisher]
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Abstract Carr-Purcell-Meiboom-Gill relaxation dispersion (CPMG RD) NMR spectroscopy has emerged as a powerful tool for quantifying the kinetics and thermodynamics of millisecond time-scale exchange processes involving the interconversion between a visible ground state and one or more minor, sparsely populated invisible â??excitedâ?? conformational states. Recently it has also become possible to determine atomic resolution...
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Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Photosynth Res. 2011 Aug 13;
Authors: Pandit A, de Groot HJ
This short review describes how solid-state NMR has provided a mechanistic and electronic picture of pigment-protein and pigment-pigment interactions in photosynthetic antenna complexes. NMR results on purple bacterial antenna complexes show how the packing of the protein and the pigments inside the light-harvesting oligomers induces mutual...
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First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
First solid-state NMR analysis of uniformly (13)C-enriched major light-harvesting complexes from Chlamydomonas reinhardtti and identification of protein and cofactor spin clusters.
Biochim Biophys Acta. 2011 Jan 25;
Authors: Pandit A, Morosinotto T, Reus M, Holzwarth AR, Bassi R, de Groot HJ
The light-harvesting complex II (LHCII) is the main component of the...
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[NMR paper] Biosynthetic site-specific (13) C labeling of the light-harvesting 2 protein complex:
Biosynthetic site-specific (13) C labeling of the light-harvesting 2 protein complex: a model for solid state NMR structure determination of transmembrane proteins.
Related Articles Biosynthetic site-specific (13) C labeling of the light-harvesting 2 protein complex: a model for solid state NMR structure determination of transmembrane proteins.
J Biomol NMR. 2004 Nov;30(3):267-74
Authors: van Gammeren AJ, Hulsbergen FB, Hollander JG, de Groot HJ
Partly biosynthetic site-directed isotopically (13)C enriched photosynthetic light-harvesting...
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11-24-2010 10:03 PM
[NMR paper] Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Related Articles Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Nat Struct Biol. 1998 Aug;5(8):692-7
Authors: Fraenkel E, Pabo CO
Homeodomains are one of the key families of eukaryotic DNA-binding motifs and provide an important model system for studying protein-DNA interactions. We have crystallized the Antennapedia homeodomain-DNA complex and solved this structure at 2.4 A resolution. NMR and molecular dynamics studies...
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[NMR paper] Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynt
Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynthetic reaction centers from multispin pheophytin enrichment and 2-D 13C MAS NMR dipolar correlation spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynthetic reaction centers from multispin pheophytin enrichment and 2-D 13C MAS NMR dipolar correlation spectroscopy.
Biochemistry. 1997 Jun 17;36(24):7513-9
Authors: ...
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[NMR paper] Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynt
Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynthetic reaction centers from multispin pheophytin enrichment and 2-D 13C MAS NMR dipolar correlation spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Characterization of pheophytin ground states in Rhodobacter sphaeroides R26 photosynthetic reaction centers from multispin pheophytin enrichment and 2-D 13C MAS NMR dipolar correlation spectroscopy.
Biochemistry. 1997 Jun 17;36(24):7513-9
Authors: ...
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[NMR paper] A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus me
A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin.
Eur J Biochem. 1990 Aug 28;192(1):225-9
Authors: Yamamoto Y, Osawa A, Inoue Y, Chûjô R, Suzuki T
The ferric high-spin form of the myoglobin from the shark Galeorhinus japonicus, which...
An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
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