scholarly journals Thiol and Mn(2+)-mediated oxidation of veratryl alcohol by horseradish peroxidase

1991 ◽  
Vol 266 (22) ◽  
pp. 14288-14293
Author(s):  
J.P. McEldoon ◽  
J.S. Dordick
2001 ◽  
Vol 265 (3) ◽  
pp. 1008-1014 ◽  
Author(s):  
Rimko Ten Have ◽  
Robbert G. De Thouars ◽  
Henk J. Swarts ◽  
Jim A. Field

1997 ◽  
Vol 66 (1) ◽  
pp. 65-71 ◽  
Author(s):  
Takahiro Yamamoto ◽  
Yasushi Maeda ◽  
Seiichi Matsugo ◽  
Hiromi Kitano

2010 ◽  
Vol 17 (4) ◽  
pp. 356-362 ◽  
Author(s):  
Min Zhu ◽  
Xue-Mei Huang ◽  
Han-Xi Shen

1993 ◽  
Vol 293 (2) ◽  
pp. 431-435 ◽  
Author(s):  
P Ander ◽  
G Sena-Martins ◽  
J C Duarte

Reduction of H2O2-oxidized manganese peroxidase (MnP), lignin peroxidase and, to some extent, horseradish peroxidase, was studied in the presence of cellobiose oxidase (CbO) and cellobiose. It was found that the reversion rates for MnP compound II and lignin peroxidase compound II back to native enzymes increased significantly in the presence of CbO and cellobiose. However, the reduction of cytochrome c by CbO plus cellobiose was 40 times faster than the reduction of MnP compound II. Also, the lag phase before reversion to the native states decreased for all three peroxidases in the presence of CbO and cellobiose. Active CbO did not repress formation of compounds I or II of the peroxidases, and Mn2+/veratryl alcohol reduced compound II of the peroxidases much more rapidly than did active CbO. This indicates that, in the presence of Mn2+ or veratryl alcohol, MnP and lignin peroxidase can complete their catalytic cycles and function normally without interference from CbO. Without the presence of peroxidase substrates, active CbO reduced compound II of the above peroxidases.


2001 ◽  
Vol 66 (4) ◽  
pp. 663-675 ◽  
Author(s):  
Markéta Mikšanová ◽  
Jiří Hudeček ◽  
Jan Páca ◽  
Marie Stiborová

Thein vitroenzymatic metabolism of a recalcitrant dye Remazol Brilliant Blue R (RBBR) was investigated using horseradish peroxidase (HRP). At optimum pH (4.5), the apparent Michaelis constant (KM) value for the oxidation of RBBR catalyzed by HRP is 14.8 μmol l-1. HRP-mediated conversion of RBBR proceedsviaa conventional peroxidase reaction, by a sequential one-electron oxidation of two molecules of RBBR by the peroxidase Compounds I and II. The oxidation is inhibited by radical trapping agents (nicotinamide adenine dinucleotide reduced (NADH), ascorbate, glutathione). This confirms that the peroxidase-mediated oxidation of RBBR proceedsviaradical mechanism. Gel permeation profile of the RBBR oxidation products shows that the pattern of molecular weight distribution was shifted to the higher molecular weight region indicating formation of RBBR oligomers. In addition to HRP, the RBBR dye is also oxidized by another peroxidase, the mammalian lactoperoxidase.


2007 ◽  
Vol 35 (2) ◽  
pp. 126-135 ◽  
Author(s):  
V. Vojinović ◽  
R.H. Carvalho ◽  
F. Lemos ◽  
J.M.S. Cabral ◽  
L.P. Fonseca ◽  
...  

2016 ◽  
Vol 190 ◽  
pp. 127-145 ◽  
Author(s):  
Majd Eshtaya ◽  
Andinet Ejigu ◽  
Gill Stephens ◽  
Darren A. Walsh ◽  
George Z. Chen ◽  
...  

Environmental concerns have brought attention to the requirement for more efficient and renewable processes for chemicals production. Lignin is the second most abundant natural polymer, and might serve as a sustainable resource for manufacturing fuels and aromatic derivatives for the chemicals industry after being depolymerised. In this work, the mediator 2,2′-azino-bis(3-ethylbenthiazoline-6-sulfonic acid) diammonium salt (ABTS), commonly used with enzyme degradation systems, has been evaluated by means of cyclic voltammetry (CV) for enhancing the oxidation of the non-phenolic lignin model compound veratryl alcohol and three types of lignin (organosolv, Kraft and lignosulfonate) in the ionic liquid 1-ethyl-3-methylimidazolium ethyl sulfate, ([C2mim][C2SO4]). The presence of either veratryl alcohol or organosolv lignin increased the second oxidation peak of ABTS under select conditions, indicating the ABTS-mediated oxidation of these molecules at high potentials in [C2mim][C2SO4]. Furthermore, CV was applied as a quick and efficient way to explore the impact of water in the ABTS-mediated oxidation of both organosolv and lignosulfonate lignin. Higher catalytic efficiencies of ABTS were observed for lignosulfonate solutions either in sodium acetate buffer or when [C2mim][C2SO4] (15 v/v%) was present in the buffer solution, whilst there was no change found in the catalytic efficiency of ABTS in [C2mim][C2SO4]–lignosulfonate mixtures relative to ABTS alone. In contrast, organosolv showed an initial increase in oxidation, followed by a significant decrease on increasing the water content of a [C2mim][C2SO4] solution.


2001 ◽  
Vol 84 (3-4) ◽  
pp. 279-286 ◽  
Author(s):  
Nelson Durán ◽  
Natália Bromberg ◽  
Airton Kunz

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