Co5V2(P2O7)4 was crystallized by chemical vapour transport using HCl as transport agent. Its crystal structure is isotypic to that of Fe(II) 5Fe(III) 2(P2O7)4 and can be regarded as a member of the thortveitite structure family with corrugated layers of metal-oxygen polyhedra extending parallel to (010). Significant occupational disorder between cobalt(II) and vanadium(III) is observed. Four of...

Reducing hexaazatrinaphthylene (HAN) with potassium in the presence of 18-c-6 produces [{K(18-c-6)}HAN], which contains the S=1/2 radical [HAN](.-) . The [HAN](.-) radical can be transferred to the cobalt(II) amide [Co{N(SiMe3 )2 }2 ], forming [K(18-c-6)][(HAN){Co(N'')2 }3 ]; magnetic measurements on this compound reveal an S=4 spin system with strong cobalt-ligand antiferromagnetic exchange an...

In the title tris-(pyrazol-yl)borate (Tp(Ph2)) complex, [NiBr(C(45)H(34)BN(6))], the Ni, Br and B atoms lie on a crystallographic threefold axis and a distorted NiN(3)Br tetra-hedral geometry arises for the metal ion. In the crystal, C-H⋯(C=C) and C-H⋯π inter-actions help to establish the polar crystal packing.

In the title compound, [ZnBr(C(4)H(8)N(2)S)(3)]Br, the Zn(II) atom is coordinated by one Br atom and the S atoms of three N-allyl-thio-urea ligands in a distorted tetra-hedral geometry. The Zn(II) atom and the two Br atoms are located on a threefold axis.

The trinuclear title compound, [Co(3)(CH(3)COO)(4)(C(20)H(22)N(2)O(6))(2)]·2CH(2)Cl(2), contains mixed-valence cobalt ions in the following order Co(III)-Co(II)-Co(III) where all the three cobalt ions are hexa-coordinated. The central cobalt ion is situated on an inversion centre and is in an all-oxygen environment, coordinated by four phenolate O atoms and two O atoms from bridging acetate gro...

Inhibition of prolyl hydroxylase domain-containing protein (PHD) by hypoxia stabilizes hypoxia-inducible factor 1 and increases the expression of target genes, such as vascular endothelial growth factor. Although the systemic renin-angiotensin system is activated by hypoxia, the role of PHD in the regulation of the renin-angiotensin system remains unknown. We examined the effect of PHD inhibiti...

Inhibition of prolyl hydroxylase domain-containing protein (PHD) by hypoxia stabilizes hypoxia-inducible factor 1 and increases the expression of target genes, such as vascular endothelial growth factor. Although the systemic renin-angiotensin system is activated by hypoxia, the role of PHD in the regulation of the renin-angiotensin system remains unknown. We examined the effect of PHD inhibiti...