Probing the electronic structure of a copper(ii) complex by CW- and pulse-EPR spectroscopy

2017 ◽  
Vol 46 (26) ◽  
pp. 8458-8475 ◽  
Author(s):  
Zoi G. Lada ◽  
Yiannis Sanakis ◽  
Catherine P. Raptopoulou ◽  
Vassilis Psycharis ◽  
Spyros P. Perlepes ◽  
...  

The electronic structure of a mononuclear octahedral copper(ii) complex has been studied using CW EPR spectroscopy and other advanced methods including Davies ENDOR and HYSCORE (1H and 13C) spectroscopy.

Author(s):  
Yujeong Kim ◽  
Jin Kim ◽  
Linh. K. Nguyen ◽  
Yong-Min Lee ◽  
Wonwoo Nam ◽  
...  

Multifrequency, multitechnique pulse EPR spectroscopy was employed to unravel the spin Hamiltonian parameters of 17O in the [FeV=O] moiety with two different tetraamido macrocyclic ligands (TAMLs), [FeV(O)(TAML-1)]– (1, H4(TAML-1) =...


Author(s):  
Aidin R. Balo ◽  
Lizhi Tao ◽  
R. David Britt

AbstractOwing to their importance, diversity and abundance of generated paramagnetic species, radical S-adenosylmethionine (rSAM) enzymes have become popular targets for electron paramagnetic resonance (EPR) spectroscopic studies. In contrast to prototypic single-domain and thus single-[4Fe–4S]-containing rSAM enzymes, there is a large subfamily of rSAM enzymes with multiple domains and one or two additional iron–sulfur cluster(s) called the SPASM/twitch domain-containing rSAM enzymes. EPR spectroscopy is a powerful tool that allows for the observation of the iron–sulfur clusters as well as potentially trappable paramagnetic reaction intermediates. Here, we review continuous-wave and pulse EPR spectroscopic studies of SPASM/twitch domain-containing rSAM enzymes. Among these enzymes, we will review in greater depth four well-studied enzymes, BtrN, MoaA, PqqE, and SuiB. Towards establishing a functional consensus of the additional architecture in these enzymes, we describe the commonalities between these enzymes as observed by EPR spectroscopy.


Author(s):  
Nikolay G. Maksimov ◽  
Victor V. Verpekin ◽  
Dmitry V. Zimonin ◽  
Galina V. Burmakina ◽  
Oleg S. Chudin ◽  
...  

The chemical oxidation of the cluster CpReFePt(μ3-C=CHPh)(CO)5(dppe) (Cp = η5-C5H5, dppe = η2- Ph2P(CH2)2PPh2) resulted in a radical cation [CpReFePt(μ3-C=CHPh)(CO)5(dppe)]+• that is sufficiently stable only at low temperature. An electronic structure of the radical cation was studied by EPR and following parameters were obtained by comparison of the experimental and model spectrum: gx = 2.070 gy = 2.0295 gz = 1.997; Ax(31P) = 17 Ay(31P) = 49 Az(31P) = 35 (Gs);Ax(195Pt) = 62 Ay(195Pt) = 45 Az(195Pt) = 105 (Gs). An unpaired electron is seen to be mainly concentrated on the iron atom (85-90%) and partially on the platinum atom (10-15%). Further transformation of the radical cation led to the formation of the binuclear complex Cp(CO)2RePt(μ-C=CHPh)(dppe) and the Fe-carbonyl fragment


2012 ◽  
Vol 376 (32) ◽  
pp. 2195-2199 ◽  
Author(s):  
Pengbo Feng ◽  
Ya Wang ◽  
Xing Rong ◽  
Ji-Hu Su ◽  
Chenyong Ju ◽  
...  

2016 ◽  
Vol 7 (5) ◽  
pp. 3172-3180 ◽  
Author(s):  
Karin Halbmair ◽  
Jan Seikowski ◽  
Igor Tkach ◽  
Claudia Höbartner ◽  
Deniz Sezer ◽  
...  

Distance measurements in RNAs by pulse EPR with TEMPO-labeled nucleotides allow for model free conversion of distances into base-pair separation.


2020 ◽  
Vol 22 (7) ◽  
pp. 3875-3882
Author(s):  
Arpad Mihai Rostas ◽  
Loic Ledernez ◽  
Lisa Dietel ◽  
Lorenz Heidinger ◽  
Michael Bergmann ◽  
...  

A nitrogen plasma generated by a self-designed microplasma device was analyzed by cw and pulse EPR spectroscopy in real time. Nitrogen atoms were detected and characterized in terms of spectral widths, relaxation times and actual concentrations.


2015 ◽  
Vol 3 (17) ◽  
pp. 4352-4358 ◽  
Author(s):  
Dongming Zhou ◽  
Kevin R. Kittilstved

The ground state electronic structure of Fe3+ dopants in colloidal ZnO nanocrystals is studied by EPR spectroscopy and reveals multiple Fe3+ coordination environments during nanocrystal growth.


Biochemistry ◽  
2008 ◽  
Vol 47 (25) ◽  
pp. 6637-6649 ◽  
Author(s):  
Yuk-Ki Lee ◽  
Mei M. Whittaker ◽  
James W. Whittaker

Biochemistry ◽  
2011 ◽  
Vol 50 (34) ◽  
pp. 7390-7404 ◽  
Author(s):  
Troy A. Stich ◽  
Gregory J. Yeagle ◽  
Rachel J. Service ◽  
Richard J. Debus ◽  
R. David Britt

2002 ◽  
Vol 106 (10) ◽  
pp. 2801-2811 ◽  
Author(s):  
Jeffrey Harmer ◽  
Sabine Van Doorslaer ◽  
Igor Gromov ◽  
Martin Bröring ◽  
Gunnar Jeschke ◽  
...  

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