MAS NMR structure refinement of uniformly 13C enriched chlorophyll a/water aggregates with 2D dipolar correlation spectroscopy

Boender, Gert Jan; Raap, J.; Prytulla, S.; Oschkinat, Hartmut; Groot, Huub J. M. de

doi:10.1016/0009-2614(95)00357-a

Cited by 53 publications

(93 citation statements)

References 19 publications

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“…The spectra were recorded by using 2.0-ms ramped cross polarization and two-pulse phase modulation decoupling during acquisition (18,19). Radio frequency-driven dipolar recoupling correlation spectra were acquired by using a pathway-selective phase cycling method (20). The 2D heteronuclear correlation spectra were obtained with phase-modulated Lee-Goldburg decoupling during the t 1 period (21,22).…”

Section: Methodsmentioning

confidence: 99%

¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

Creemers

Kiihne

Bovée-Geurts

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

120

184

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Rhodopsin is a member of the superfamily of G-protein-coupled receptors. This seven ␣-helix transmembrane protein is the visual pigment of the vertebrate rod photoreceptor cells that mediate dim light vision. In the active binding site of this protein the ligand or chromophore, 11-cis-retinal, is covalently bound via a protonated Schiff base to lysine residue 296. Here we present the complete 1 H and 13 C assignments of the 11-cis-retinylidene chromophore in its ligand-binding site determined with ultra high field magic angle spinning NMR. Native bovine opsin was regenerated with 99% enriched uniformly 13 C-labeled 11-cis-retinal. From the labeled pigment, 13 C carbon chemical shifts could be obtained by using two-dimensional radio frequency-driven dipolar recoupling in a solid-state magic angle spinning homonuclear correlation experiment.

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Section: Methodsmentioning

confidence: 99%

¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

Creemers

Kiihne

Bovée-Geurts

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

120

184

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“…It is obvious that this approximation must break down nances and improvement of resolution in modern multidiwhen the magnetic field is sufficiently strong. It has been mensional high-resolution solid-state NMR (1,2). For inproposed that the dipolar interactions are effectively trunstance, structure refinement of large solid-type biological cated by the chemical shift in high fields, yielding narrower preparations using 2-D homonuclear 13 C dipolar-correlation 1 H lines (16).…”

mentioning

confidence: 99%

High Magnetic Field for Enhanced Proton Resolution in High-Speed CP/MAS Heteronuclear1H–13C Dipolar-Correlation Spectroscopy

Rossum

Boender

Groot

1996

Journal of Magnetic Resonance, Series A

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“…Our earlier MAS NMR studies of chlorosomes from Chlorobaculum tepidum showed that NMR signals from chlorosomes are almost exclusively due to the self-aggregated BChls. [17,36] Thus, we attribute the response after deuteration in Figure 4B to the self-assembled BChl e, with a minor contribution from the residual H 2 O in the buffer. The wPMLG-5 spectrum for the BChl e response from the chlorosomes in deuterated buffer is shown in Figure 4C.…”

Section: Resultsmentioning

confidence: 94%

wPMLG‐5 Spectroscopy of Self‐Aggregated BChl e in Natural Chlorosomes of Chlorobaculum Limnaeum

Miloslavina

Gupta

Tank

et al. 2014

Israel Journal of Chemistry

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1H magic angle spinning (MAS) nuclear magnetic resonance (NMR), employing rapid spinning and the wPMLG‐5 pulse sequence, was used to explore the possibility for performing 1H solid state NMR of a light‐harvesting organelle, the chlorosome antenna of Chlorobaculum limnaeum. This natural antenna system is built from bacteriochlorophyll e (BChl e) molecules that are self‐assembled to form a supramolecular scaffold for in vivo harvesting of light. We present preliminary data on this chlorosome species and address the feasibility of performing wPMLG spectroscopy, in terms of high power irradiation on a fragile biological sample. In parallel, enhancing the 1H shift dispersion from the magnetic field can help to resolve signals from protons that resonate downfield. Different line narrowing mechanisms operating in parallel provide access to resolving selected 1H signals collected from the moderately sized and chemically diverse BChl e molecular motif in the chlorosome scaffold. These discoveries will be helpful for future studies of structural and functional characteristics of self‐assembled natural and artificial light‐harvesting molecules.

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MAS NMR structure refinement of uniformly 13C enriched chlorophyll a/water aggregates with 2D dipolar correlation spectroscopy

Cited by 53 publications

References 19 publications

¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

High Magnetic Field for Enhanced Proton Resolution in High-Speed CP/MAS Heteronuclear1H–13C Dipolar-Correlation Spectroscopy

wPMLG‐5 Spectroscopy of Self‐Aggregated BChl e in Natural Chlorosomes of Chlorobaculum Limnaeum

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MAS NMR structure refinement of uniformly 13C enriched chlorophyll a/water aggregates with 2D dipolar correlation spectroscopy

Cited by 53 publications

References 19 publications

1 H and 13 C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

1 H and 13 C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

High Magnetic Field for Enhanced Proton Resolution in High-Speed CP/MAS Heteronuclear1H–13C Dipolar-Correlation Spectroscopy

wPMLG‐5 Spectroscopy of Self‐Aggregated BChl e in Natural Chlorosomes of Chlorobaculum Limnaeum

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Product

Resources

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¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin

¹ H and ¹³ C MAS NMR evidence for pronounced ligand–protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin