593-15-7

Usage

Uses

Used in Industrial Applications:
1,8-Difluorooctane is used as a solvent for various industrial applications due to its non-flammability, low toxicity, and chemical stability.
Used in Analytical Chemistry:
1,8-Difluorooctane is used as a test compound for evaluating the performance of analytical instruments and methods, particularly in the field of chromatography.
Used in Pharmaceutical and Agrochemical Production:
1,8-Difluorooctane is utilized in the production of pharmaceuticals and agrochemicals, contributing to the development of various products in these industries.
However, it is important to note that the environmental impact and potential toxicity of 1,8-Difluorooctane require careful handling and disposal to prevent harm to human health and the ecosystem.

InChI:InChI=1/C8H16F2/c9-7-5-3-1-2-4-6-8-10/h1-8H2

Upstream product

• 111-20-6 1,10-decanedioic acid 
• 629-41-4 1,8-Octanediol 

Relevant academic research and scientific papers

Tuning the regio- and stereoselectivity of C-H activation in n-octanes by cytochrome P450 BM-3 with fluorine substituents: Evidence for interactions between a C-F bond and aromatic π systems

We employed the water- soluble cytochrome P450 BM-3 to study the activity and regiospecificity of oxidation of fluorinated n-octanes. Three mutations, A74G, F87V, and L188Q, were introduced into P450 BM-3 to allow the system to undergo n-octane oxidation. In addition, the alanine at residue 328 was replaced with a phenylalanine to introduce an aromatic residue into the hydrophobic pocket to examine whether or not van der Waals interactions between a C-F substituent in the substrate and the polarizable π system of the phenylalanine may be used to steer the positioning of the substrate within the active-site pocket of the enzyme and control the regioselectivity and stereoselectivity of hydroxylation. Interestingly, not only was the regioselectivity controlled when the fluorine substituent was judiciously positioned in the substrate, but the electron input into the iron-heme group became tightly coupled to the formation of product, essentially without abortive side reactions. Remarkable enhancement of the coupling efficiency between electron input and product formation was observed for a range of fluorinated octanes in the enzyme even without the A328F mutation, presumably because of interactions of the C-F substituent with the π system of the porphyrin macrocycle within the active-site pocket. Evidently, tightening the protein domain containing the heme pocket tunes the distribution of accessible enzyme conformations and the associated protein dynamics that activate the iron porphyrin for substrate hydroxylation to allow the reactions mediated by the high-valent FeIV=O to become kinetically more commensurate with electron transfer from the flavin adenine dinucleotide (FAD)/flavin mononucleotide (FMN) reductase. These observations lend compelling evidence to support significant van der Waals interactions between the CF2 group and aromatic π systems within the heme pocket when the fluorinated octane substrate is bound. Activation of F-octanes: Cytochrome P450 BM-3-A74GF87VL188Q (see figure) and the A328F variant regionselectively converted fluorinated C8 alkanes to the corresponding secondary alcohols. The pattern of reactivity, especially the unprecedented regio- and stereoselectivity, observed for 4,4-difluorooctane suggested that specific interactions of the fluorinated substituent with aromatic π systems within the active site could tune the reactivity. Copyright