DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis

Hannah Russell; Rachel Stewart; Christopher Prior; Vasily S. Oganesyan; Thembaninkosi G.  Gaule; Janet E. Lovett

doi:10.1007/s00723-021-01321-6

DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis

Hannah Russell, Rachel Stewart, Christopher Prior, Vasily S. Oganesyan, Thembaninkosi G. Gaule, Janet E. Lovett

Research output: Contribution to journal › Article › peer-review

Abstract

In 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.

Original language	English
Number of pages	21
Journal	Applied Magnetic Resonance
Volume	First Online
Early online date	29 Mar 2021
DOIs	https://doi.org/10.1007/s00723-021-01321-6
Publication status	E-pub ahead of print - 29 Mar 2021

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@article{b667cc4d736646278b5e17c6f7b6ac03,

title = "DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis",

abstract = "In 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.",

author = "Hannah Russell and Rachel Stewart and Christopher Prior and Oganesyan, {Vasily S.} and Gaule, {Thembaninkosi G.} and Lovett, {Janet E.}",

note = "Authors acknowledge financial support from EPSRC (studentship to HR EP/R513337/1, Grant support to VSO EP/P007554/1, Grant support to TGG EP/L015005/1), The Royal Society (URF to JEL URF150698), and The Wellcome Trust for a multi-user equipment grant (099149/Z/12/Z).",

year = "2021",

month = mar,

day = "29",

doi = "10.1007/s00723-021-01321-6",

language = "English",

volume = "First Online",

journal = "Applied Magnetic Resonance",

issn = "0937-9347",

publisher = "Springer",

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TY - JOUR

T1 - DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis

AU - Russell, Hannah

AU - Stewart, Rachel

AU - Prior, Christopher

AU - Oganesyan, Vasily S.

AU - Gaule, Thembaninkosi G.

AU - Lovett, Janet E.

N1 - Authors acknowledge financial support from EPSRC (studentship to HR EP/R513337/1, Grant support to VSO EP/P007554/1, Grant support to TGG EP/L015005/1), The Royal Society (URF to JEL URF150698), and The Wellcome Trust for a multi-user equipment grant (099149/Z/12/Z).

PY - 2021/3/29

Y1 - 2021/3/29

N2 - In 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.

AB - In 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.

UR - https://link.springer.com/article/10.1007%2Fs00723-021-01321-6#Sec19

U2 - 10.1007/s00723-021-01321-6

DO - 10.1007/s00723-021-01321-6

M3 - Article

SN - 0937-9347

VL - First Online

JO - Applied Magnetic Resonance

JF - Applied Magnetic Resonance

ER -

DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis

Abstract

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State of the art pulse EPR instrumentati: State of the art pulse EPR instrumentation for long range distance measurements in biomacromolecules