Discovery and characterization of oxidative biocatalysts : styrene monooxygenase, putrescine oxidase, and alditol oxidase

Dit document is (ook) beschikbaar voor ruilverkeer - alleen door bibliotheken -. [Bestelformulier]

Redox enzymes catalyze electron transfer from one substrate to another, usually with the help of an enzyme-bound cofactor. These cofactors can be organic molecules (e.g. NAD, FAD, and PQQ), metals (e.g. Cu, Fe, and Zn), or metal complexes like heme or iron-sulphur clusters. Some cofactors are tightly or even covalently bound to the enzyme, forming an intrinsic part of the active site. This type of cofactor is called a prosthetic group. Enzymes of which the prosthetic group is lost or removed are called apo enzymes and are catalytically inactive. Cofactors which are not permanently bound to the enzyme, but enter and leave the active site to facilitate catalysis are often referred to as coenzymes. Since coenzymes are usually oxidized or reduced when they leave the enzyme, they can also be regarded as cosubstrates. NADH and NADPH are well-known coenzymes of oxidative enzymes.
This thesis will focus on oxidative enzymes that act on organic molecules and employ molecular oxygen as oxidant. All studied enzymes utitlize a FAD flavin cofactor to assist in the oxidation reactions.

Meer informatie in de catalogus
Meer informatie in Picarta