Stereogenic boron in 2-amino-1,1-diphenylethanol-based boronate–imine and amine complexes

Beilstein Journal of Organic Chemistry ◽

10.3762/bjoc.7.72 ◽

2011 ◽

Vol 7 ◽

pp. 615-621 ◽

Cited By ~ 3

Author(s):

Sebastian Schlecht ◽

Walter Frank ◽

Manfred Braun

Keyword(s):

Crystal Structure ◽

Boron Atom ◽

The Novel ◽

Amine Complexes ◽

Amine Complex ◽

Boron Center

Racemic boronate–imine and boronate–amine complexes 8 and 10, both featuring a stereogenic boron atom were synthesized from 2-amino-1,1-diphenylethanol (5) and characterized by crystal structure analyses. Proof of enantiomerism at the boron center for the novel boronate–amine complex 10 was established by separation of the enantiomers. Racemization barriers were found to be in the same range for both amine and imine complexes (100–110 kJ/mol).

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Some Novel Cobalt Diphenylphosphine Complexes: Synthesis, Characterization, and Behavior in the Polymerization of 1,3-Butadiene

Molecules ◽

10.3390/molecules26134067 ◽

2021 ◽

Vol 26 (13) ◽

pp. 4067

Author(s):

Giovanni Ricci ◽

Giuseppe Leone ◽

Giorgia Zanchin ◽

Benedetta Palucci ◽

Alessandra Forni ◽

...

Keyword(s):

Crystal Structure ◽

Single Crystals ◽

The Novel ◽

X Ray Diffraction ◽

X Ray ◽

And Behavior

Some novel cobalt diphenylphosphine complexes were synthesized by reacting cobalt(II) chloride with (2-methoxyethyl)diphenylphosphine, (2-methoxyphenyl)diphenylphosphine, and 2-(1,1-dimethylpropyl)-6-(diphenylphosphino)pyridine. Single crystals suitable for X-ray diffraction studies were obtained for the first two complexes, and their crystal structure was determined. The novel compounds were then used in association with methylaluminoxane (MAO) for the polymerization of 1,3-butadiene, and their behavior was compared with that exhibited in the polymerization of the same monomer by the systems CoCl2(PnPrPh2)2/MAO and CoCl2(PPh3)2/MAO. Some significant differences were observed depending on the MAO/Co ratio used, and a plausible interpretation for such a different behavior is proposed.

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The preparation of zinc(II) and cadmium(II) complexes of the pentadentate N3S2 ligand formed from 2,6-diacetylpyridine and S-benzyldithiocarbazate (H2SNNNS) and the X-ray crystal structure of the novel dimeric [Zn2(SNNNS)2] complex

Polyhedron ◽

10.1016/j.poly.2003.08.004 ◽

2003 ◽

Vol 22 (27) ◽

pp. 3433-3438 ◽

Cited By ~ 38

Author(s):

Mohammad Akbar Ali ◽

A.H Mirza ◽

C.W Voo ◽

Ai Ling Tan ◽

P.V Bernhardt

Keyword(s):

Crystal Structure ◽

The Novel ◽

X Ray

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Reaction ofortho-Methylbenzonitrile with LithiumN,N,N′-Trimethylethylenediamide: Assembly and Crystal Structure of a Primary Isoquinolinoamidolithium–Secondary Amine Complex

European Journal of Inorganic Chemistry ◽

10.1002/(sici)1099-0682(199807)1998:7<879::aid-ejic879>3.0.co;2-v ◽

1998 ◽

Vol 1998 (7) ◽

pp. 879-883 ◽

Cited By ~ 7

Author(s):

Neil Feeder ◽

Ronald Snaith ◽

Andrew E. H. Wheatley

Keyword(s):

Crystal Structure ◽

Secondary Amine ◽

Amine Complex

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Crystal Structure of the Streptomyces coelicolor Sortase E1 Transpeptidase Provides Insight into the Binding Mode of the Novel Class E Sorting Signal

PLoS ONE ◽

10.1371/journal.pone.0167763 ◽

2016 ◽

Vol 11 (12) ◽

pp. e0167763 ◽

Cited By ~ 11

Author(s):

Michele D. Kattke ◽

Albert H. Chan ◽

Andrew Duong ◽

Danielle L. Sexton ◽

Michael R. Sawaya ◽

...

Keyword(s):

Crystal Structure ◽

Streptomyces Coelicolor ◽

Binding Mode ◽

The Novel ◽

Sorting Signal ◽

Insight Into ◽

Class E

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Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19–CDC5L complex

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s139900471303318x ◽

2014 ◽

Vol 70 (3) ◽

pp. 780-788 ◽

Cited By ~ 2

Author(s):

Jae-Woo Ahn ◽

Sangwoo Kim ◽

Eun-Jung Kim ◽

Yeo-Jin Kim ◽

Kyung-Jin Kim

Keyword(s):

Crystal Structure ◽

The Novel ◽

Molecular Architecture ◽

Repeat Protein ◽

Binding Partner ◽

Catalytic Activation ◽

Repeat Structure ◽

Repeat Domain ◽

Importin Α ◽

Structural Insights

The hPrp19–CDC5L complex plays a crucial role during human pre-mRNA splicing by catalytic activation of the spliceosome. In order to elucidate the molecular architecture of the hPrp19–CDC5L complex, the crystal structure of CTNNBL1, one of the major components of this complex, was determined. Unlike canonical ARM-repeat proteins such as β-catenin and importin-α, CTNNBL1 was found to contain a twisted and extended ARM-repeat structure at the C-terminal domain and, more importantly, the protein formed a stable dimer. A highly negatively charged patch formed in the N-terminal ARM-repeat domain of CTNNBL1 provides a binding site for CDC5L, a binding partner of the protein in the hPrp19–CDC5L complex, and these two proteins form a complex with a stoichiometry of 2:2. These findings not only present the crystal structure of a novel ARM-repeat protein, CTNNBL1, but also provide insights into the detailed molecular architecture of the hPrp19–CDC5L complex.

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