Reactions of Palladium Chloride with Amino Spirocyclic Cyclotriphosphazenes: Isolation and Crystal Structures of Novel Mono- and Bimetallic Complexes Formed by the Hydrolysis of a .lambda.5-Diazaphospholane Ring

1994 ◽  
Vol 33 (14) ◽  
pp. 3085-3090 ◽  
Author(s):  
A. Chandrasekaran ◽  
S. S. Krishnamurthy ◽  
M. Nethaji
1993 ◽  
Vol 48 (10) ◽  
pp. 1411-1418 ◽  
Author(s):  
Hermann Irngartinger ◽  
Jochen Lichtenthäler ◽  
Dieter Fenske ◽  
Gerhard Baum

The 2,5-bis(2-arylvinyl)-1,4-benzoquinones 1a-1e are formed from hydrolysis of their corresponding ketals 5 which are generated by anodic oxidation of the corresponding 1,4-dimethoxybenzene derivatives 4. The crystal structures of the quinone compounds 1a, 1d and 1e have been determined by X-ray analyses. The bond lengths of the quinone system are influenced by polar resonance structures. An α-type packing mode is observed for the three crystal structures of compounds 1. The vinylic double bonds have short intermolecular distances (1a: 4.417(5), 1d: 3.653(2), 1e: 4.224(5) Å). Only the crystals of 1d with the shortest contacts are photoreactive


2007 ◽  
Vol 60 (19) ◽  
pp. 2035-2044 ◽  
Author(s):  
Ahmet Karadağ ◽  
Ahmet Bulut ◽  
Ayşegül Şenocak ◽  
İbrahim Uçar ◽  
Orhan Büyükgüngör

2019 ◽  
Vol 116 (21) ◽  
pp. 10360-10365 ◽  
Author(s):  
Rishi Arora ◽  
Amitabh V. Nimonkar ◽  
Daniel Baird ◽  
Chunhua Wang ◽  
Chun-Hao Chiu ◽  
...  

Lipoprotein lipase (LPL) plays a central role in triglyceride (TG) metabolism. By catalyzing the hydrolysis of TGs present in TG-rich lipoproteins (TRLs), LPL facilitates TG utilization and regulates circulating TG and TRL concentrations. Until very recently, structural information for LPL was limited to homology models, presumably due to the propensity of LPL to unfold and aggregate. By coexpressing LPL with a soluble variant of its accessory protein glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) and with its chaperone protein lipase maturation factor 1 (LMF1), we obtained a stable and homogenous LPL/GPIHBP1 complex that was suitable for structure determination. We report here X-ray crystal structures of human LPL in complex with human GPIHBP1 at 2.5–3.0 Å resolution, including a structure with a novel inhibitor bound to LPL. Binding of the inhibitor resulted in ordering of the LPL lid and lipid-binding regions and thus enabled determination of the first crystal structure of LPL that includes these important regions of the protein. It was assumed for many years that LPL was only active as a homodimer. The structures and additional biochemical data reported here are consistent with a new report that LPL, in complex with GPIHBP1, can be active as a monomeric 1:1 complex. The crystal structures illuminate the structural basis for LPL-mediated TRL lipolysis as well as LPL stabilization and transport by GPIHBP1.


1985 ◽  
Vol 4 (12) ◽  
pp. 2201-2206 ◽  
Author(s):  
Gerald. Doyle ◽  
Kenneth A. Eriksen ◽  
Donna. Van Engen

Polyhedron ◽  
2009 ◽  
Vol 28 (12) ◽  
pp. 2397-2402 ◽  
Author(s):  
Tamara R. Todorović ◽  
Urszula Rychlewska ◽  
Beata Warżajtis ◽  
Dušanka D. Radanović ◽  
Nenad R. Filipović ◽  
...  

1983 ◽  
Vol 251 (3) ◽  
pp. 281-287 ◽  
Author(s):  
William Clegg ◽  
Martin Haase ◽  
Uwe Klingebiel ◽  
Jutta Neemann ◽  
George M. Sheldrick

1977 ◽  
Vol 32 (12) ◽  
pp. 1361-1364 ◽  
Author(s):  
Brigitte Knopp ◽  
Klaus-Peter Lörcher ◽  
Joachim Strähle

The partial hydrolysis of AsPh4[MoNCl4] (AsPh4 = [(C6H5)4As]) leads to AsPh4[MoOCl4]. Both salts crystallize isotypic in the tetragonal space group P 4/n with Z = 2. The crystal structures are built up by AsPh4 cations and square pyramidal [MoXCl4] anions with the symmetry C4v. The Mo—N distance of 166 pm and the slightly longer Mo-O distance of 171 pm indicate strong π-bonding.


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