Vares T , Lundell TK & Hatakka A ( 1992 ) Novel heme-containing enzyme possibly involved in lignin degradation by the white-rot fungus Junghuhnia separabilima . FEMS Microbiol Lett 99 : 53 – 58 .Vares T., Lundell T.K., Hatakka A.I. : Novel heme-containing enzyme possibly ...
Background: Chloroperoxidase (CPO) is a versatile heme-containing enzyme that exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzym...
In the final enzymatic step (step 8), ferrous iron is incorporated into the PP-IX ring to form heme-b by the enzyme ferrochelatase (FECH) on the matrix side of the inner mitochondrial membrane [58,59]. FECH consists of a homodimer, with each subunit containing and...
In this mechanism, the enzyme reacts with one equivalent of H2O2to give [Fe4+=O]R' (compound I). This is a two-electron oxidation/reduction reaction where H2O2is reduced to water and the enzyme is oxidised. One oxidising equivalent resides on iron, giving the oxyferryl[1]intermediate, w...
Horseradish peroxidase (HRP) mediates efficient conversion of many phenolic contaminants and thus has potential applications for pollution control. Such potentially important applications suffer however from the fact that the enzyme becomes quickly inact
Under the same conditions, TvDyP1 retained 20 to 80% of its enzyme activity. The two proteins were catalytically characterized, and TvVP2 was shown to accept a wider range of reducing substrates than TvDyP1. Furthermore, both enzymes were found to be active against two flavonoids, quercetin...
Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl-) and hydrogen peroxide (H2O2). It is implicate... D Maitra,F Shaeib,I Abdulhamid,... - 《Free Radical Biology & Medicine》 被引量: 45发表: 2013年 Heme-Protein Interaction in My...
However, P450 classes have been discovered in which the redox partners are fused to the heme domain of the enzyme, creating multicomponent, self-sufficient systems. These are attractive biocatalysts, as the need for identification and expression of separate redox partners is obviated. Structural data...
We found that the addition of a large amount of butyraldoxime (final concentration, 200 mM) to ferrous OxdA with a low enzyme concentration (final concentration, 5 μM) yields a longlived OxdA-substrate complex (named OS-II), whose UV-vis spectrum is different from the corresponding ...
A heme-C-containing enzyme complex that exhibits nitrate and nitrite reductase activity from the dissimilatory iron-reducing bacterium Geobacter metallired... Nitrate reduction in the dissimilatory iron-reducing bacterium Geobacter metallireducens was investigated. Nitrate reductase and nitrite reductase activi...