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  • Blackwell Publishing Ltd  (6)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 92 (1992), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Cellobiose oxidase activity from Phanerochaete chrysosporium was monitored continuously by two techniques that are independent of the presence of a solid substrate, measuring either ferricyanide by the electrode potential of anaerobic ferricyanide plus ferrocyanide, or O2 with a specific electrode. Both methods demonstrated that microcrystalline cellulose (Avicel) is a substrate for oxidation. All experiments were at pH 4.0 and 30°C. Rates were evaluated for two-electron transfer. For Avicel → ferricyanide, a study of initial rates gave kcat= 0.40 ± 0.05 s−1, much slower than kcat= 3.6 ± 0.3 s−1 with cellobiose as substrate. With Avicel plus 0.2 μM cellobiose oxidase, the rate fell to half its initial value in 3–8 min, indicating a heterogeneity of reducing ends. For Avicel → O2, kcat= 0.057 ± 0.004 s−1. Half maximal rates corresponded to Km(Avicel) = 8 ± 2 gl−1 with ferricyanide, and 3.3 ± 0.5 gl−1 with O2 as acceptor.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology reviews 13 (1994), S. 0 
    ISSN: 1574-6976
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract: Many forms of Fe(II) react with H202 to generate hydroxyl radicals (Fenton reaction). There is evidence that hydroxyl radicals are important in brown-rot, while they can be formed by secondary reactions during lignin breakdown by white-rot fungi. Their involvement in cellulose breakdown creates a range of oxidized sugars. The two reactants of Fenton's reagent can be generated by Fe(II) autoxidation, or by superoxide in reaction with Fe(III). A rapid autoxidation is not possible for complexes with a high Fe(III)/Fe(II) redox potential. Turning to specific pathways for formation of Fenton's reagent, decomposition of Fe(III)-oxalate is probably solely a photochemical process. Lignin peroxidases can act indirectly as a source of superoxide, either by reactions that lead to a peroxyradical, or by 1-electron oxidation of an aliphatic compound creating a strong reductant. Cellobiose dehydrogenase can provide a direct enzymic source for Fenton's reagent (S.M. Kremer and P.M. Wood (1992) Eur. J. Biochem. 208, 807–814). In the experiments as published, hydroxyl radical production was limited by the slow interaction of cellobiose dehydrogenase with O2. This limitation can be removed by the presence of an iron complex with an autoxidizable Fe(lI) state. The successful use of Fenton's reagent by a living organism requires a spatial separation between initiating enzyme(s) and the site of production of hydroxyl radicals. The mobility of the extra electron on Fe(II) by intermolecular transfer may be important for achieving this separation.
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 7 (1980), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 33 (1986), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Ten redox reagents have been tested as electron donors to ammonia monooxygenase in whole cells of Nitrosomonas europaea. Positive results were obtained with tri- and tetramethylhydroquinone. An earlier study showed that phenol was converted into hydroquinone by the monooxygenase. Cells were therefore incubated with trimethylphenol, to see if its hydroxylation to trimethylhydroquinone would lead to a self-sufficient conversion of trimethylphenol into trimethylquinone. No trimethylquinone could be detected. The maximal rates of propene epoxidation obtained with tri-and tetramethylhydroquinone were 1.8 and 4.6 μmol · h−1· mg protein−1, respectively.
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 145 (1996), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Cellobiose dehydrogenase was purified from the brown rot fungus Coniophora puteana. Strong cross-reaction was observed with antibodies to cellobiose:quinone oxidoreductase from the white rot fungus Phanerochaete chrysosporium. Kinetic measurements were made with cellobiose as electron donor. Ferricyanide and DCPIP both showed a pH optimum close to pH 4, but activity with ferricyanide declined more rapidly when the pH was raised. Dioxygen reduction to hydrogen peroxide was observed, but at a much lower rate than for other acceptors. These properties are similar to those of cellobiose dehydrogenase from P. chrysosporium, despite differences between brown and white rot modes of decay.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 20 (1983), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Membranes from Nitrosomonas europaea were found to contain two b-type cytochromes. One had an α-band centred at 562 nm and Em,7=+ 155 mV; the other had an α-band maximum close to 558 nm and Em,7=+ 40 mV. A b-type cytochrome ran at an apparent Mr of 32000 on lithium dodecyl sulphate/polyacrylamide gels at 4°C.
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