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Mekanismer for brun- og hvidmuld svampes nedbrydning af tr - Nature

Mekanismer for brun- og hvidmuld svampes nedbrydning af tr - Nature

Mekanismer for brun- og hvidmuld svampes nedbrydning af tr - Nature

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oxidation <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> et givet subs<strong>tr</strong>atet er de samme, uanset peroxidasens eller oxi-<br />

dasens redox potentiale, under <s<strong>tr</strong>ong>for</s<strong>tr</strong>ong>udsætning <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> at dette er højere end sub-<br />

s<strong>tr</strong>atets. [Kersten P.J. et al. (1990)].<br />

Tabel 10<br />

Lignin peroxidase (H8/H 2 O 2 ), peberrod peroxidase (horseradish peroxidase, HRP/H 2 O 2 ) <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong><br />

laccase’s evnen til oxidation <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> 12 metoxybenzen congenerer med redox potentialer spændende<br />

fra 0,81 til 1,76 V. [Kersten P.J. et al. (1990)]<br />

(+) indikerer oxidation <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> <s<strong>tr</strong>ong>for</s<strong>tr</strong>ong>bindelsen<br />

(-) indikerer mangel på oxidation <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> <s<strong>tr</strong>ong>for</s<strong>tr</strong>ong>bindelsen.<br />

(±) indikerer oxidation <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> <s<strong>tr</strong>ong>for</s<strong>tr</strong>ong>bindelse, men med hurtig inaktivering <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> enzym.<br />

(‡) indikerer direkte detektion <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> kation radikal.<br />

Ma n g a n a f h æ n g i g PE r o x i d a s E<br />

Mangan<s<strong>tr</strong>ong>af</s<strong>tr</strong>ong>hængig peroxidase (MnP, EC 1.11.1.13) er ligesom LiP en oxi-<br />

doreductase hvor oxidanten er hydr<s<strong>tr</strong>ong>og</s<strong>tr</strong>ong>en peroxid. Transkriptionen <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> mnp<br />

genet reguleres koncen<strong>tr</strong>ations- <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> vekstfase <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong>hængigt <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> Mn(II). mnp mRNA<br />

produceres kun under sekundær vækstfase <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> koncen<strong>tr</strong>ationen topper ved<br />

180 μM Mn(II) i mediet <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> kan ikke erstattes <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> hverken Fe, Zn, Co, Cu eller Ni<br />

[Brown J.A. et al. (1991)].<br />

Som medlem <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> samme heme peroxidase familie som LiP, er mange <s<strong>tr</strong>ong>af</s<strong>tr</strong>ong> MnP’s<br />

s<strong>tr</strong>ukturelle egenskaber de samme som LiP. MnP er krystall<s<strong>tr</strong>ong>og</s<strong>tr</strong>ong>r<s<strong>tr</strong>ong>af</s<strong>tr</strong>ong>isk bestemt<br />

<s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> indeholder samme domæner, ferroprotoporphyrin <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> His s<strong>tr</strong>uktur som LiP.<br />

MnP har ligesom LiP 4 tilstands<s<strong>tr</strong>ong>for</s<strong>tr</strong>ong>mer, en fuldt reduceret hviletilstand MnP, to<br />

oxiderede tilstande MnP-I <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> MnP-II, <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> en katalytiks inaktiv tilstand MnP-III.<br />

MnP er et monomer glucoprotein med en pI på ca. 4,5 <s<strong>tr</strong>ong>og</s<strong>tr</strong>ong> en molekylevægt på<br />

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