Polarized Crystal Spectra of Tris (2,2'-bipyridine)copper(II), -nickel(II), -cobalt(II), -iron(II), and -ruthenium(II),
Tris(2,2′-bipyridine)ruthenium(II) hexafluorophosphate …
Full spectral data for all compounds, together with novel data for ruthenium tris (4-methyl-4′-vinyl-2,2′-bipyridine) bis (hexafluorophosphate), are reported.">
Thus, upon complexation to form ruthenium tris (4-methyl-4′-vinyl-2,2′-bipyridine) bis (hexafluorophosphate), the bis-, mono- and non-vinyl complexes were also present.
Tris(bipyridine)ruthenium(II) chloride | Wiki | Everipedia
Electropolymerisation of ruthenium tris (4-methyl-4′-vinyl-2,2′-bipyridine) bis (hexafluorophosphate) to produce a high quality polymer film requires the maximum number of vinyl ligands per molecule of complex.
Full spectral data for all compounds, together with novel data for ruthenium tris (4-methyl-4′-vinyl-2,2′-bipyridine) bis (hexafluorophosphate), are reported.
Tris(bipyridine)ruthenium(II) dichloride is the with the formula [Ru(bipy)3]Cl2. This orange crystalline salt is obtained as the , although all of the properties of interest are in the [Ru(bipy)3]2+, which has received much attention because of its distinctive optical properties. The chlorides can be replaced with other , such as .
Highly functionalised ruthenium(II) tris-bipyridine receptor 1 which acts as a selective sensor for equine cytochrome c (cyt c) is shown to destabilise the native protein conformation by around 25 °C. Receptors 2 and 3 do not exert this effect confirming the behaviour is a specific effect of molecular recognition between 1 and cyt c, whilst the absence of a destabilising effect on 60% acetylated cyt c demonstrates the behaviour of 1 to be protein specific. Molecular recognition also modifies the conformational properties of the target protein at room temperature as evidenced by ion-mobility spectrometry (IMS) and accelerated trypsin proteolysis.
Tris(bipyridine)ruthenium(II) chloride is the ..
> Synthesis of Tris(2,2'-bipyridine)ruthenium(II) Tetrafluoroborate
Novel synthesis and characterisation of ruthenium tris …
Tris(bipyridine)ruthenium(II) chloride : Wikis (The Full …
TRIS(2,2'-BIPYRIDYL)RUTHENIUM(II) CHLORIDE HEXAHYDRATE …
A Tris(bipyridine)ruthenium(II)–β ..
Ruthenium(II) Tris-Bipyridine Complexes With A [60 ..
We, and others– previously reported a series of ruthenium-based receptors for protein-surface recognition. Our studies have illustrated that the sensing of proteins can be performed by following the emission of the ruthenium tris-bipyridine core and that selective recognition of equine cytochrome c (cyt c) can be achieved in comparison to a series of other proteins. Furthermore, we have shown that the affnity towards protein targets is dependent upon the geometrical arrangement of ligands around the ruthenium core (fac/mer). The current paper describes our studies on the effect that binding of these receptors has on the conformational stability of cyt c. We illustrate that receptor 1 specifically destabilizes cyt c and does so in a potent and dose dependent manner, recreating some of the essential features of chaperones.
Tris(bipyridine)ruthenium(II) chloride explained
The synthesis and binding affnities of ruthenium(II) tris bipyridine receptors 1–3 have been previously reported (). Briefly, receptor 1 was shown to bind selectively to cyt c with nanomolar affnity, Kd ~ 2 nM (pH 7.4, 5 mM sodium phosphate) as evidenced by luminescence quenching upon titration of the ruthenium-based receptor with cyt c. The interaction was shown to be specific and selective as evidenced by the absence of binding towards 60% acetylated cyt c (Kd > 30 μM) and much weaker binding towards lysozyme – a protein of comparable pI/surface composition (Kd ~ 294 nM) under the conditions of the experiment. Compound 2 was shown to bind cyt c with much lower affnity (Kd ~ 23 nM) whereas compound 3, which is charge mismatched with the target protein, did not bind (Kd > 30 μM) as predicted. Experimental data point to an interaction of 1 with the haem exposed edge of cyt c; notably, a large reduction in the rate of ascorbate oxidation is observed consistent with blocking the approach of this small reducing agent. This is additionally supported by the aforementioned titration with 60% acetylated cyt c; this randomly acetylated protein preparation has its surface exposed basic residues capped by the acetyl modification and is therefore incapable of participating in strong electrostatic interactions. The majority of lysine residues in cyt c surround the haem exposed edge ().
Ruthenium(III) chloride - Wikipedia
Synthesis, Characterization, and Spectroscopic and Electrochemical Properties of New Bidentate Ligands Derived from Lysine and Cysteine and Their Complexes with Bis(2,2‘-bipyridine)ruthenium(II)
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