scholarly journals A model for random chain complexes

Author(s):  
Michael J. Catanzaro ◽  
Matthew J. Zabka
Keyword(s):  
2017 ◽  
Vol 46 (17) ◽  
pp. 5546-5557 ◽  
Author(s):  
Arunpatcha Nimthong-Roldán ◽  
Jesse L. Guillet ◽  
James McNeely ◽  
Tarik J. Ozumerzifon ◽  
Matthew P. Shores ◽  
...  

Four new quasi-1D Ni2lantern chain complexes of the form [Ni2(SOCR)4(L)]∞were prepared withN,N′-donor bridging ligands pyrazine and DABCO.


2006 ◽  
Vol 45 (19) ◽  
pp. 7722-7735 ◽  
Author(s):  
Mihail Atanasov ◽  
Peter Comba ◽  
Sebastian Förster ◽  
Gerald Linti ◽  
Thomas Malcherek ◽  
...  

Author(s):  
Aimin Xu

Let [Formula: see text] be either the category of [Formula: see text]-modules or the category of chain complexes of [Formula: see text]-modules and [Formula: see text] a cofibrantly generated hereditary abelian model structure on [Formula: see text]. First, we get a new cofibrantly generated model structure on [Formula: see text] related to [Formula: see text] for any positive integer [Formula: see text], and hence, one can get new algebraic triangulated categories. Second, it is shown that any [Formula: see text]-strongly Gorenstein projective module gives rise to a projective cotorsion pair cogenerated by a set. Finally, let [Formula: see text] be an [Formula: see text]-module with finite flat dimension and [Formula: see text] a positive integer, if [Formula: see text] is an exact sequence of [Formula: see text]-modules with every [Formula: see text] Gorenstein injective, then [Formula: see text] is injective.


2014 ◽  
Vol 205 (4) ◽  
pp. 511-524 ◽  
Author(s):  
Markus Hildenbeutel ◽  
Eric L. Hegg ◽  
Katharina Stephan ◽  
Steffi Gruschke ◽  
Brigitte Meunier ◽  
...  

Mitochondrial respiratory chain complexes convert chemical energy into a membrane potential by connecting electron transport with charge separation. Electron transport relies on redox cofactors that occupy strategic positions in the complexes. How these redox cofactors are assembled into the complexes is not known. Cytochrome b, a central catalytic subunit of complex III, contains two heme bs. Here, we unravel the sequence of events in the mitochondrial inner membrane by which cytochrome b is hemylated. Heme incorporation occurs in a strict sequential process that involves interactions of the newly synthesized cytochrome b with assembly factors and structural complex III subunits. These interactions are functionally connected to cofactor acquisition that triggers the progression of cytochrome b through successive assembly intermediates. Failure to hemylate cytochrome b sequesters the Cbp3–Cbp6 complex in early assembly intermediates, thereby causing a reduction in cytochrome b synthesis via a feedback loop that senses hemylation of cytochrome b.


2020 ◽  
Vol 44 (6) ◽  
pp. 2408-2413 ◽  
Author(s):  
Shao-Liang Zhang ◽  
Shan-Shan Li ◽  
Su-Yuan Zeng ◽  
Yang Shi ◽  
Da-Qi Wang ◽  
...  

Two new chain complexes consisting of a Mn(salen) building block bridged by O–Se–O units, [Mn2(salen)2(L)](ClO4) (1) and {[Mn(salen)]2(L)2}·Y (2) (salen = N,N′-bis(salicylidene)-ethylenediamine, L = 3,4,5-trifluorobenzeneseleninic acid, Y = salicylaldehyde) have been synthesized and characterized structurally and magnetically.


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