[NMR paper] Assignment of NMR resonances of protons covalently bound to photochemically active cofactors in photosynthetic reaction centers by 13C–1H photo-CIDNP MAS-J-HMQC experiment
Assignment of NMR resonances of protons covalently bound to photochemically active cofactors in photosynthetic reaction centers by 13C–1H photo-CIDNP MAS-J-HMQC experiment
Author(s): Pavlo Bielytskyi, Daniel Gräsing, Stefan Zahn, Kaustubh R. Mote, A. Alia, P.K. Madhu, Jörg Matysik
Abstract
Modified versions of through-bond heteronuclear correlation (HETCOR) experiments are presented to take advantage of the light-induced hyperpolarization that occurs on 13C nuclei due to the solid-state photochemically induced dynamic nuclear polarization (photo-CIDNP) effect. Such 13C–1H photo-CIDNP MAS-J-HMQC and photo-CIDNP MAS-J-HSQC experiments are applied to acquire the 2D 13C–1H correlation spectra of selectively 13C-labeled photochemically active cofactors in the frozen quinone-blocked photosynthetic reaction center (RC) of the purple bacterium Rhodobacter (R.) sphaeroides wild-type (WT). Resulting spectra contain no correlation peaks arising from the protein backbone, which greatly simplifies the assignment of aliphatic region. Based on the photo-CIDNP MAS-J-HMQC NMR experiment, we obtained assignment of selective 1H NMR resonances of the cofactors involved in the electron transfer process in the RC and compared them with values theoretically predicted by density functional theory (DFT) calculation as well as with the chemical shifts obtained from monomeric cofactors in the solution. We also compared proton chemical shifts obtained by photo-CIDNP MAS-J-HMQC experiment under continuous illumination with the ones obtained in dark by classical cross-polarization (CP) HETCOR. We expect that the proposed approach will become a method of choice for obtaining 1H chemical shift maps of the active cofactors in photosynthetic RCs and will aid the interpretation of heteronuclear spin-torch experiments.
[NMR paper] 13C->1H transfer of light-induced hyperpolarization allows for selective detection of protons in frozen photosynthetic reaction center
13C->1H transfer of light-induced hyperpolarization allows for selective detection of protons in frozen photosynthetic reaction center
Publication date: Available online 8 June 2018
Source:Journal of Magnetic Resonance</br>
Author(s): Pavlo Bielytskyi, Daniel Gräsing, Kaustubh R. Mote, Karthick Babu Sai Sankar Gupta, Shimon Vega, P.K. Madhu, A. Alia, Jörg Matysik</br>
In the present study, we exploit the light-induced hyperpolarization occurring on 13C nuclei due to the solid-state photochemically induced dynamic nuclear polarization (photo-CIDNP)...
[NMR paper] Photochemically Induced Dynamic Nuclear Polarization Observed by Solid-state NMR in a Uniformly (13)C-isotope Labeled Photosynthetic Reaction Center.
Photochemically Induced Dynamic Nuclear Polarization Observed by Solid-state NMR in a Uniformly (13)C-isotope Labeled Photosynthetic Reaction Center.
Related Articles Photochemically Induced Dynamic Nuclear Polarization Observed by Solid-state NMR in a Uniformly (13)C-isotope Labeled Photosynthetic Reaction Center.
J Phys Chem B. 2015 Jun 25;
Authors: Paul S, Bode BE, Matysik J, Alia A
Abstract
A sample of solubilized and quinone-depleted reaction centers (RC) from the purple bacterium Rhodobacter (R.) sphaeroides wild-type (WT)...
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06-26-2015 09:55 PM
Bacteriopheophytin a in the active branch of the reaction center of rhodobacter sphaeroides is not disturbed by the protein matrix as shown by 13C photo-CIDNP MAS NMR
From The DNP-NMR Blog:
Bacteriopheophytin a in the active branch of the reaction center of rhodobacter sphaeroides is not disturbed by the protein matrix as shown by 13C photo-CIDNP MAS NMR
Sai Sankar Gupta, K.B., et al., Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter sphaeroides Is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR. The Journal of Physical Chemistry B, 2013. 117(12): p. 3287-3297.
http://www.ncbi.nlm.nih.gov/pubmed/23452037
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06-22-2013 01:40 AM
[NMR paper] Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
Bacteriopheophytin a in the Active Branch of the Reaction Center of Rhodobacter Sphaeroides is Not Disturbed by the Protein Matrix as Shown by 13C Photo-CIDNP MAS NMR.
J Phys Chem B. 2013 Mar 1;
Authors: Sai Sankar Gupta KB, Alia A, Buda F, de Groot HJ, Matysik J
Abstract
The electronic structure of bacteriopheophytin a (BPhe a), the primary electron acceptor (?A) in...
Assignment of NMR resonances of protons covalently bound to photochemically active cofactors in photosynthetic reaction centers by 13C–1H photo-CIDNP MAS-J-HMQC experiment
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