Hydroxylated derivatives of coenzyme Q1 as ligands for complexation of transition metals

Mitreska, Nikolina and Mirceski, Valentin and Gulaboski, Rubin (2014) Hydroxylated derivatives of coenzyme Q1 as ligands for complexation of transition metals. In: SOE DAAD Workshop - Polymers, 5-10 Sept 2014, Ohrid, Macedonia.

[thumbnail of Book of Abstracts SOE DAAD Polymers Ohrid 2014.pdf]
Book of Abstracts SOE DAAD Polymers Ohrid 2014.pdf

Download (3MB) | Preview


Coenzymes Q (CoQ) are omnipresent molecules in livi
ng systems, which in addition to being
members of mitochondrial respiratory chain, possess
several other functions of great importance for
the cellular metabolism. They are among the most ap
pealing redox active quinone derivatives. In
mammals, the predominant homologue is CoQ
10 (ubiquinone). Unlike CoQ10 which is lipophilic, its analogue CoQ1 is much more hydrophilic, because
contains only one instead of 10 isoprenoid groups i
n the tail. The main purpose of using CoQ1 was to
serve as a model for exploring redox properties of
CoQ group in aqueous medium.
In an alkaline medium, CoQ1 s can be hydroxylated at the quinoid ring. The chemical transformations of CoQ1
in an alkaline medium has been studied by means of
cyclic and square-wave voltammetry and it is showed that upon substitution of methoxy groups, hydroxylated derivatives of CoQ1 are formed. The new hydroxilated derivatives exhibit distinct redox properties compared to the parent compound, as well as a profound complexing a
ctivity of transition metal cations such as Fe3+
and Co2+.
Besides application of electrochemical techniques,
to confirm further the chemical reaction and
the structural changes of CoQ1
in a strong alkaline medium and to investigate the
complexing activity of metal cations, a set of spectroscopic experiments has been performed

Item Type: Conference or Workshop Item (Lecture)
Subjects: Medical and Health Sciences > Basic medicine
Natural sciences > Chemical sciences
Divisions: Faculty of Medical Science
Depositing User: Rubin Gulaboski
Date Deposited: 22 Sep 2014 14:27
Last Modified: 22 Sep 2014 14:27
URI: https://eprints.ugd.edu.mk/id/eprint/10997

Actions (login required)

View Item View Item