Results 211 to 220 of about 26,797 (254)
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Thermodynamics of Binding of the Distal Calcium to Manganese Peroxidase
Biochemistry, 1997We previously demonstrated that manganese peroxidase from Phanerochaete chrysosporiumwas susceptible to thermal inactivation due to release of the distal calcium, which maintained the distal heme environment of the enzyme [Sutherland, G. R. J., Zapanta, L. S., Tien, M., & Aust, S. D. (1997) Biochemistry 36, 3654-3662]. In this investigation the binding
G R, Sutherland, S D, Aust
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Enzymatic hydrolysis of corn stover lignin by laccase, lignin peroxidase, and manganese peroxidase
Bioresource Technology, 2022Lignin of high purity and structural integrity was isolated from the enzymatic residue of corn stover. Degradation of the lignin by laccase, lignin peroxidase, and manganese peroxidase was investigated. Structural changes in the lignin after degradation were characterized by scanning electron microscopy, nitrogen adsorption and Fourier transform ...
Sitong, Zhang +7 more
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Lignin peroxidases can also oxidize manganese
Biochemistry, 1995The peroxidase isozymes secreted by the white rot fungus Phanerochaete chrysosporium include lignin peroxidases and manganese-dependent peroxidases. The major isozymes, called lignin peroxidases, are thought to oxidize chemicals directly. The manganese-dependent peroxidases (H3, H4, H5, and H9) are relatively minor, making up only a fraction of the ...
A, Khindaria, D P, Barr, S D, Aust
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The Effect of Manganese on the Oxidation of Chemicals by Lignin Peroxidase
Biochemistry, 1995It has recently been discovered that lignin peroxidase isozyme H2 (LiPH2) has the ability to oxidize Mn2+ (Khindaria et al., 1995). Furthermore, at pH 4.5, the physiological pH of Phanerochaete chrysosporium, LiPH2 oxidizes Mn2+ at a much faster rate (25 times) than veratryl alcohol (VA).
G R, Sutherland +3 more
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Manganese peroxidase-catalyzed oxidative degradation of vanillylacetone
Chemosphere, 2008When 4-(4-hydroxy-3-methoxy-phenyl)-2-butanone (vanillylacetone) was tested for manganese peroxidase (MnP)-catalyzed oxidation, it was found to be degraded with the cleavage of an aromatic ring. Among numerous products of vanillylacetone oxidation, four major ones were purified by thin-layer chromatography and identified using mass spectroscopy (MS ...
Sangpill, Hwang +3 more
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Manganese‐Substituted Carbonic Anhydrase as a New Peroxidase
Chemistry – A European Journal, 2006AbstractCarbonic anhydrase is a zinc metalloenzyme that catalyzes the hydration of carbon dioxide to bicarbonate. Replacing the active‐site zinc with manganese yielded manganese‐substituted carbonic anhydrase (CA[Mn]), which shows peroxidase activity with a bicarbonate‐dependent mechanism.
Krzysztof, Okrasa, Romas J, Kazlauskas
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Manganese, Mn-dependent peroxidases, and the biodegradation of lignin
Biochemical and Biophysical Research Communications, 1988Manganese and Mn-dependent peroxidases have been implicated in the enzymatic degradation of lignin. However, the specific role of manganese is uncertain. We report here the novel observation that in the absence of enzyme, suitably chelated Mn3+ is a ligninolytic agent capable of oxidizing veratryl alcohol, lignin model compounds, and lignin.
I T, Forrester +3 more
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Archives of Microbiology, 1993
In this study, a N-deregulated mutant (der8-5) of Phanerochaete chrysosporium was used as a tool to investigate the interrelationships between N, C, and Mn(II) regulation of LIP and MNP production in this organism. The results showed that LIP and MNP production by der8-5 was blocked in excess C medium but not in excess N medium.
M W, Van der Woude +2 more
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In this study, a N-deregulated mutant (der8-5) of Phanerochaete chrysosporium was used as a tool to investigate the interrelationships between N, C, and Mn(II) regulation of LIP and MNP production in this organism. The results showed that LIP and MNP production by der8-5 was blocked in excess C medium but not in excess N medium.
M W, Van der Woude +2 more
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Applied Biochemistry and Biotechnology, 1998
The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments.
D N, Thompson +3 more
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The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments.
D N, Thompson +3 more
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Haloperoxidase Activity of Manganese Peroxidase fromPhanerochaete chrysosporium
Archives of Biochemistry and Biophysics, 1997Manganese peroxidase (MnP) from Phanerochaete chrysosporium exhibits haloperoxidase activity at low pH. In the presence of hydrogen peroxide, MnP oxidizes bromide and iodide as measured by the formation of tribromide and triiodide complexes and the halogenation of various organic substrates.
D, Sheng, M H, Gold
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