Neutral or cationic arene ruthenium complexes providing both hydrophilic as well as hydrophobic properties due to the robustness of the ruthenium-arene unit hold a high potential for the development of metal-based anticancer drugs. Mononuclear arene ruthenium complexes containing P- or N-donor ligands or N,N-, N,O- or O,O-chelating ligands, dinuclear arene ruthenium systems with adjustable orga...

The ruthenium complexes are known for their anticancer property. Some ruthenium complexes can bind with protein that may be related to the anticancer activity. The protein binding features of few ruthenium complexes have been analyzed to understand the amino acid selectivity within protein sequences. The docking, Molecular mechanics and QM/MM methods are used to predict the binding sites of the...

Sarcoplasmic reticulum Ca(2+)-ATPase has previously been shown to bind and dissociate two Ca2+ ions in a sequential mode. This behaviour is confirmed here by inducing sequential Ca2+ dissociation with Ruthenium Red. Ruthenium Red binds to sarcoplasmic reticulum vesicles (6 nmol/mg) with a Kd = 2 microM, producing biphasic kinetics of Ca2+ dissociation from the Ca(2+)-ATPase, decreasing the affi...

BACKGROUND The new ruthenium(II)-arene complex, which bearing a carborane unit, ruthenium and ferrocenyl functional groups, has a novel versatile synthetic chemistry and unique properties of the respective material at the nanoscale level. The ruthenium(II)-arene complex shows significant cytotoxicity to cancer cells and tumor-inhibiting properties. However, ruthenium(II)-arene complex of mechan...

The effects of ruthenium red and the related compounds tetraamine palladium (4APd) and tetraamine platinum (4APt) were studied on the ryanodine activated Ca2+ release channel reconstituted in planar bilayers with the immunoaffinity purified ryanodine receptor. Ruthenium red, applied at submicromolar concentrations to the myoplasmic side (cis), induced an all-or-none flickery block of the ryanod...

Ruthenium myoglobins have been prepared by the reconstitution of horse heart apomyoglobin with either ruthenium(I1) or ruthenium(II1) mesoporphyrin IX (MpIX) derivatives. The ruthenium(I1) and -(III) myoglobins (RuMb and RuMb+, respectively) contain one ruthenium porphyrin/heme binding site; the species are readily interconverted using dithionite for reduction and bromine for oxidation. RuMb bi...

Three new ruthenium amidinate complexes were prepared: tris(diisopropylacetamidinato)-ruthenium(III), Ru(iPrNC(Me)NiPr)3 4; bis(diisopropyl-acetamidinato)ruthenium(II) dicarbonyl, Ru( iPrNC(Me)NiPr)2(CO)2 5; and bis(ditert-butylacetamidinato)ruthenium(II) dicarbonyl, Ru(tBuNC(Me)NtBu)2(CO)2 6. They have been synthesized and characterized by H NMR, TG and X-ray structure analysis. These three co...

The hydroxido-bridged dinuclear ruthenium complex 4, which is supported by Tp ligands, has been prepared from protonation of the oxido-bridged dinuclear ruthenium complex 3. Additional protonation of 4, affording the aqua-bridged dinuclear ruthenium complex 5 in situ, and subsequent treatment with NO gave rise to the dicationic dinitrosyl complex 2. These indicate completion of the NO reduction...

In 1981 Pecoraro and Chianelli reported a complete study of catalytic behavior of transition metal sulfides catalysts in hydrodesulfurization (HDS) of dibenzothiophene (DBT) [1], in which was found a periodic tendency of the metallic sulfides activity, where ruthenium sulfide showed the highest HDS activity. These results were corroborated later by Raje et al. [2] and Liaw et al. [3], further s...

Ruthenium myoglobins have been prepared by the reconstitution of horse heart apomyoglobin with either ruthenium(II) or ruthenium(III) mesoporphyrin IX (MpIX) derivatives. The ruthenium(II) and -(III) myo globins (RuMb and RuMb+, respectively) contain one ruthenium porphyrin/heme binding site; the species are readily interconverted using dithionite for reduction and bromine for oxidation. RuMb b...