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Thiocyanate complexes are not widely used commercially. Possibly the oldest application of thiocyanate complexes was the use of thiocyanate as a test for ferric ions in aqueous solution. [15] The reverse was also used: testing for the presence of thiocyanate by the addition of ferric salts. The 1:1 complex of thiocyanate and iron is deeply red.
Thiocyanate shares its negative charge approximately equally between sulfur and nitrogen. As a consequence, thiocyanate can act as a nucleophile at either sulfur or nitrogen—it is an ambidentate ligand. [SCN] − can also bridge two (M−SCN−M) or even three metals (>SCN−
In methyl thiocyanate, N≡C and C−S distances are 116 and 176 pm. By contrast, N=C and C=S distances are 117 and 158 pm in isothiocyanates. [7] Typical bond angles for C−S−C are 100°. [3] By contrast C−N=C in aryl isothiocyanates is 165°. Again, the thiocyanate isomers are quite different with C−S−C angle near 100°.
It is formed when an oxygen is singly bonded to the thiocyanate group. Hypothiocyanous acid is a fairly weak acid; its acid dissociation constant (pK a) is 5.3. Hypothiocyanite is formed by peroxidase [1] catalysis of hydrogen peroxide and thiocyanate: H 2 O 2 + SCN − → OSCN − + H 2 O
Mercury(II) thiocyanate (Hg(SCN) 2) is an inorganic chemical compound, the coordination complex of Hg 2+ and the thiocyanate anion. It is a white powder. It is a white powder. It will produce a large, winding "snake" when ignited, an effect known as the Pharaoh's serpent .
Copper(I) thiocyanate is a hole conductor, a semiconductor with a wide band gap (3.6 eV, therefore transparent to visible and near infrared light). [11] It is used in photovoltaics in some third-generation cells as a hole transfer layer.
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A thiocyanate hydrolase (EC 3.5.5.8) is an enzyme belonging to the family of hydrolases. The systematic name of this enzyme class is thiocyanate aminohydrolase. This enzyme catalyzes the chemical reaction: SCN − + 2 H 2 O + H + ⇌ SCO + NH 3. The mechanism is proposed to involve a metal thiocyanate complex.