New method of characterizing slow‐tumbling motions for nitroxide spin labels/probes from second‐derivative ESR powder spectra

1982 ◽  
Vol 76 (2) ◽  
pp. 805-808 ◽  
Author(s):  
Sook Lee ◽  
D. P. Ames ◽  
I. M. Brown
Keyword(s):  
New Method ◽  
Spin Labels ◽  
Second Derivative ◽  
Nitroxide Spin Labels

scholarly journals DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis

2021 ◽  
Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Amine Oxidase ◽  
Spin Labels ◽  
Arthrobacter Globiformis ◽  
Copper Amine Oxidase ◽  
Dipole Interactions ◽  
Nitroxide Spin Labels ◽  
Double Electron Electron Resonance ◽  
Dipolar Modulation ◽  
Paramagnetic Centres

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.

Comparison of Ionic and Non-Ionic Nitroxide Spin Labels for Urographic Enhancement in Magnetic Resonance Imaging

1987 ◽  
Vol 28 (5) ◽  
pp. 593-600 ◽  
Author(s):  
Wolfgang Grodd ◽  
H. Paajanen ◽  
U. G. Eriksson ◽  
D. Revel ◽  
F. Terrier ◽  
...  
Keyword(s):  
Magnetic Resonance Imaging ◽  
Magnetic Resonance ◽  
Spin Labels ◽  
Resonance Imaging ◽  
Nitroxide Spin Labels

Pulsed electron–electron double resonance: beyond nanometre distance measurements on biomacromolecules

2011 ◽  
Vol 434 (3) ◽  
pp. 353-363 ◽  
Author(s):  
Gunnar W. Reginsson ◽  
Olav Schiemann
Keyword(s):  
Protein Complexes ◽  
Double Resonance ◽  
Resonance Method ◽  
Spin Labels ◽  
Coupling Mechanism ◽  
Distance Measurements ◽  
Paramagnetic Resonance ◽  
Distance Distributions ◽  
Nitroxide Spin Labels ◽  
Amino Acid Radicals

PELDOR (or DEER; pulsed electron–electron double resonance) is an EPR (electron paramagnetic resonance) method that measures via the dipolar electron–electron coupling distances in the nanometre range, currently 1.5–8 nm, with high precision and reliability. Depending on the quality of the data, the error can be as small as 0.1 nm. Beyond mere mean distances, PELDOR yields distance distributions, which provide access to conformational distributions and dynamics. It can also be used to count the number of monomers in a complex and allows determination of the orientations of spin centres with respect to each other. If, in addition to the dipolar through-space coupling, a through-bond exchange coupling mechanism contributes to the overall coupling both mechanisms can be separated and quantified. Over the last 10 years PELDOR has emerged as a powerful new biophysical method without size restriction to the biomolecule to be studied, and has been applied to a large variety of nucleic acids as well as proteins and protein complexes in solution or within membranes. Small nitroxide spin labels, paramagnetic metal ions, amino acid radicals or intrinsic clusters and cofactor radicals have been used as spin centres.

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