Long-range distance determination in fully deuterated RNA with pulsed EPR spectroscopy

AbstractElectron paramagnetic resonance (EPR) spectroscopy provides a variety of tools to study structures and structural changes of large biomolecules or complexes thereof. In order to unravel secondary structure elements, domain arrangements or complex formation, continuous wave and pulsed EPR methods capable of measuring the magnetic dipole coupling between two unpaired electrons can be used to obtain long-range distance constraints on the nanometer scale. Such methods yield reliably and precisely distances of up to 80 Å, can be applied to biomolecules in aqueous buffer solutions or membranes, and are not size limited. They can be applied either at cryogenic or physiological temperatures and down to amounts of a few nanomoles. Spin centers may be metal ions, metal clusters, cofactor radicals, amino acid radicals, or spin labels. In this review, we discuss the advantages and limitations of the different EPR spectroscopic methods, briefly describe their theoretical background, and summarize important biological applications. The main focus of this article will be on pulsed EPR methods like pulsed electron–electron double resonance (PELDOR) and their applications to spin-labeled biosystems.

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Long-Range Distance Measurements on Nucleic Acids in Cells by Pulsed EPR Spectroscopy

Angewandte Chemie ◽

10.1002/ange.201100886 ◽

2011 ◽

Vol 123 (22) ◽

pp. 5176-5180 ◽

Cited By ~ 38

Author(s):

Ivan Krstić ◽

Robert Hänsel ◽

Olga Romainczyk ◽

Joachim W. Engels ◽

Volker Dötsch ◽

...

Keyword(s):

Nucleic Acids ◽

Long Range ◽

Epr Spectroscopy ◽

Distance Measurements ◽

Pulsed Epr ◽

In Cells

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Faculty Opinions recommendation of Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1003875.43155 ◽

2002 ◽

Author(s):

Thorsten Dieckmann

Keyword(s):

Structural Analysis ◽

Nucleic Acids ◽

Epr Spectroscopy ◽

Metal Ion ◽

Pulsed Epr

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Aminoxyl Radicals of B/P Frustrated Lewis Pairs: Refinement of the Spin-Hamiltonian Parameters by Field- and Temperature-Dependent Pulsed EPR Spectroscopy

PLoS ONE ◽

10.1371/journal.pone.0157944 ◽

2016 ◽

Vol 11 (6) ◽

pp. e0157944 ◽

Cited By ~ 2

Author(s):

Marcos de Oliveira ◽

Robert Knitsch ◽

Muhammad Sajid ◽

Annika Stute ◽

Lisa-Maria Elmer ◽

...

Keyword(s):

Epr Spectroscopy ◽

Spin Hamiltonian ◽

Frustrated Lewis Pairs ◽

Temperature Dependent ◽

Pulsed Epr ◽

Hamiltonian Parameters ◽

Aminoxyl Radicals ◽

Lewis Pairs

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Structural Studies of Membrane Proteins using Pulsed EPR Spectroscopy

Biophysical Journal ◽

10.1016/j.bpj.2018.11.345 ◽

2019 ◽

Vol 116 (3) ◽

pp. 56a

Author(s):

Gary A. Lorigan ◽

Indra D. Sahu ◽

Daniel L. Drew ◽

Gunjan Dixit ◽

Tanbir Ahammad

Keyword(s):

Membrane Proteins ◽

Epr Spectroscopy ◽

Structural Studies ◽

Pulsed Epr

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Two-dimensional 67Zn HYSCORE spectroscopy reveals that a Zn-bacteriochlorophyll aP′ dimer is the primary donor (P840) in the type-1 reaction centers of Chloracidobacterium thermophilum

Physical Chemistry Chemical Physics ◽

10.1039/c9cp06556c ◽

2020 ◽

Vol 22 (11) ◽

pp. 6457-6467 ◽

Cited By ~ 2

Author(s):

Philip Charles ◽

Vidmantas Kalendra ◽

Zhihui He ◽

Mohammad Hassan Khatami ◽

John H. Golbeck ◽

...

Keyword(s):

Epr Spectroscopy ◽

Isotopic Labeling ◽

Reaction Centers ◽

Two Dimensional ◽

Pulsed Epr ◽

Primary Donor

Using pulsed EPR spectroscopy and isotopic labeling we demonstrate that reaction centers of Chloracidobacterium thermophilum have an unusual primary donor that is a dimer of Zn-bacteriochlorophyll aP′ molecules.

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