Quasi-isotropic SMMs: slow relaxation of the magnetization in polynuclear CuII/MnII complexes.

2022 ◽  
Author(s):  
Evangelos Pilichos ◽  
Pradip Bhunia ◽  
Merce Font-Bardia ◽  
Ashutosh Ghosh ◽  
Julia Mayans ◽  
...  

Three field induced SMMs built from quasi isotropic cations like CuII and MnII have been characterized, showing that relatively large clusters with quasi negligible D and different ground spin state,...

2003 ◽  
Vol 2003 (3) ◽  
pp. 541-555 ◽  
Author(s):  
Phalguni Chaudhuri ◽  
Eva Rentschler ◽  
Frank Birkelbach ◽  
Carsten Krebs ◽  
Eckhard Bill ◽  
...  

2018 ◽  
Vol 42 (10) ◽  
pp. 7612-7616 ◽  
Author(s):  
L. Rousseau ◽  
E. Brémond ◽  
G. Lefèvre

Factors governing the ground spin state of iron(i) complexes are analyzed by DFT methods. An efficient benchmarking procedure is reported.


1997 ◽  
Vol 323 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Johanneke L. H. BUSCH ◽  
Jacques L. BRETON ◽  
Barry M. BARTLETT ◽  
Fraser A. ARMSTRONG ◽  
Richard JAMES ◽  
...  

The 8Fe ferredoxin III from Desulfovibrio africanus is a monomeric protein which contains two [4Fe-4S]2+/1+ clusters, one of which is labile and can readily and reversibly lose one Fe under oxidative conditions to yield a [3Fe-4S]1+/0 cluster. This 4Fe cluster has an S = 3/2 ground spin state instead of S = 1/2 in the reduced +1 state [George, Armstrong, Hatchikian and Thomson (1989) Biochem. J.264, 275-284]. The co-ordination to this cluster is unusual in that an aspartate (Asp14, D14) is found where a cysteine residue normally occurs. Using a mutant protein obtained from the overexpression in Escherichia coli of a synthetic gene in which Asp14, the putative ligand to the removable Fe, has been changed to Cys, we have studied the cluster interconversion properties of the labile cluster. Analysis by EPR and magnetic-circular-dichroism spectroscopies showed that the Asp14 → Cys (D14C) mutant contains two [4Fe-4S]2+/1+ clusters, both with S = 1/2 in the reduced state. Also, unlike in native 8Fe D. africanus ferredoxin III, the 4Fe ↔ 3Fe cluster interconversion reaction was found to be sluggish and did not go to completion. It is inferred that the reversibility of the reaction in the native protein is due to the presence of the aspartate residue at position 14 and that this residue might protect the [3Fe-4S] cluster from further degradation.


2008 ◽  
pp. 2277 ◽  
Author(s):  
Stergios Piligkos ◽  
Jesper Bendix ◽  
Høgni Weihe ◽  
Constantinos J. Milios ◽  
Euan K. Brechin

2014 ◽  
Vol 126 (21) ◽  
pp. 5414-5417 ◽  
Author(s):  
Samantha A. Magee ◽  
Stephen Sproules ◽  
Anne-Laure Barra ◽  
Grigore A. Timco ◽  
Nicholas F. Chilton ◽  
...  

1962 ◽  
Vol 126 (2) ◽  
pp. 540-555 ◽  
Author(s):  
D. H. Lyons ◽  
T. A. Kaplan ◽  
K. Dwight ◽  
N. Menyuk

2006 ◽  
Vol 45 (30) ◽  
pp. 4875-4875 ◽  
Author(s):  
Ayuk M. Ako ◽  
Ian J. Hewitt ◽  
Valeriu Mereacre ◽  
Rodolphe Clérac ◽  
Wolfgang Wernsdorfer ◽  
...  
Keyword(s):  

2008 ◽  
Vol 14 (30) ◽  
pp. 9117-9121 ◽  
Author(s):  
Ross Inglis ◽  
Leigh F. Jones ◽  
Kevin Mason ◽  
Anna Collins ◽  
Stephen A. Moggach ◽  
...  

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