Resonance Raman spectra of chloroperoxidase

Champion, P. M.; Remba, R.D.; Chiang, R.; Fitchen, D. B.; Hager, Lowell P.

doi:10.1016/0005-2795(76)90015-5

Cited by 36 publications

(11 citation statements)

References 11 publications

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“…The most interesting finding in this work (King et al, 1966) was that production of oxindole mediated by the microsomal fraction would also proceed under anaerobic conditions. The physicochemical similarities between chloroperoxidase and cytochrome P-450 have been previously reported (Hollenberg & Hager, 1973;Champion et al, 1976;Makino et al, 1976;Estabrook & Werringloer, 1977). It is possible that the reactions catalysed by chloroperoxidase and cytochrome P-450 become very similar when the latter is subjected to anaerobic conditions.…”

Section: Discussionsupporting

confidence: 76%

Peroxide oxidation of indole to oxindole by chloroperoxidase catalysis

Corbett¹,

Chipko²

1979

Biochemical Journal

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In the presence of chloroperoxidase, indole was oxidized by H2O2 to give oxindole as the major product. Under most conditions oxindole was the only product formed, and under optimal conditions the conversion was quantitative. This reaction displayed maximal activity at pH 4.6, although appreciable activity was observed throughout the entire pH range investigated, namely pH 2.5-6.0. Enzyme saturation by indole could not be demonstrated, up to the limit of indole solubility in the buffer. The oxidation kinetics were first-order with respect to indole up to 8 mM, which was the highest concentration of indole that could be investigated. On the other hand, 2-methylindole was not affected by H2O2 and chloroperoxidase, but was a strong inhibitor of indole oxidation. The isomer 1-methylindole was a poor substrate for chloroperoxidase oxidation, and a weak inhibitor of indole oxidation. These results suggest the possibility that chloroperoxidase oxidation of the carbon atom adjacent to the nitrogen atom in part results from hydrogen-bonding of the substrate N-H group to the enzyme active site.

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Section: Discussionsupporting

confidence: 76%

Peroxide oxidation of indole to oxindole by chloroperoxidase catalysis

Corbett¹,

Chipko²

1979

Biochemical Journal

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“…On the other hand, horseradish peroxidase, catalase and lactoperoxidase1display the reduced CO Soret peak at 420nm (Hollenberg & Hager, 1973). Other studies of the haem moieties of chloroperoxidase and cytochrome P-450 have further demonstrated the remarkable similarities of these oxidative enzymes (Champion et al, 1976;Makino et al, 1976;Estabrook & Werringloer, 1977). Regardless of the close relationship in the active sites of these two enzymes, the oxidation of arylamines by the enzymes results in quite distinct products, with chloroperoxidase effecting an overall four-electron oxidation.…”

Section: Discussionmentioning

confidence: 89%

Chloroperoxidase-catalysed oxidation of 4-chloroaniline to 4-chloronitrosobenze

Corbett¹,

Chipko²,

Baden³

1978

Biochemical Journal

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The incubation of 4-chloroaniline with chloroperoxidase and H2O2 resulted in a rapid formation of 4-chloronitrosobenzene. This enzymic oxidation displayed a pH optimum at 4.4 with a Km of 8.1x10(-4)M and catalytic-centre activity of 312. The initial rate of the reaction was strongly affected by the presence of halide ions. 4-Chlorophenylhydroxylamine was even more rapidly converted into the nitroso compound. A reaction mechanism is proposed on the basis of currently accepted theory for the catalytic action of chloroperoxidae. A noteworthy aspect of this new reaction is the difference in the products previously reported for the action of classical peroxidases on anilines and the single nitroso product resulting from chloroperoxidase oxidation.

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“…3a), exhibits the same bands as in Fig. 2a, but with the modified intensity pattern intrinsic to near-ultraviolet excitation [105,107,139]. The 1374 cm À1 m 4 band that normally serves as the beacon for signal optimization with deep violet excitation ( Fig.…”

Section: Detection Of Resonance Raman Signals From Compounds I and Iimentioning

confidence: 87%