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The world of multi-copper enzymes

Groen, J (2016) The world of multi-copper enzymes. Bachelor's Thesis, Biology.

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Abstract

In this review the natural functions and reaction mechanisms of some multi-copper enzymes are described. Three multi-copper oxidases (MCOs) are describes and one reductive enzyme, nitrite reductase. The structure that all these enzyme have in common is a cupredoxin-like folded beta barrel. They all contain a T1 copper site in this beta barrel. The MCOs all contain a trinuclear copper cluster (TNC) as well, consisting of a T2 copper and a T3 copper. Nitrite reductase contains only a T2 copper instead of a TNC. In all of them electrons are accepted at the T1 copper and transferred internally to the TNC/T2 site. Here oxygen is reduced to water, in the case of MCOs, or nitrite to nitric oxide, in the case of nitrite reductase. The MCOs described are laccases, ascorbate oxidase and human ferroxidases. Laccases are found in various organisms, such as plants, bacteria and fungi. It catalyzes the oxidation of lignin-related compounds and could be involved in the depolymerisation of lignin as well. Ascorbate oxidase is found in plants, near the cell walls. It catalyzes the oxidation of ascorbate to dehydroascorbate. This reaction might be involved in the wound healing of plants. There are three types of human ferroxidases: ceruloplasmin, hephaestin and zyklopen. All of these are found in different part of the human body. They are capable of the oxidation of iron and are responsible for the iron regulation. Nitrite reductases are found in bacteria. It is involved in the respiratory chain, where it can reduce nitrite to nitric oxide, as an anaerobic alternative for oxygen. This reaction is important for the terrestrial nitrogen cycle as well. These denitrifying bacteria can be used to remove nitrite from waste- and groundwater as well.

Item Type: Thesis (Bachelor's Thesis)
Degree programme: Biology
Thesis type: Bachelor's Thesis
Language: English
Date Deposited: 15 Feb 2018 08:13
Last Modified: 15 Feb 2018 08:13
URI: http://fse.studenttheses.ub.rug.nl/id/eprint/14117

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