The oxidation of phenylhydrazine by tyrosinase

Yi Ming Sung; Srivardhan Reddy Gayam; Shu-Pao Wu

doi:10.1007/s12010-013-0165-7

The oxidation of phenylhydrazine by tyrosinase

Yi Ming Sung, Srivardhan Reddy Gayam, Shu-Pao Wu^*

^*Corresponding author for this work

Department of Applied Chemistry

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25°C). The values of k_cat and K _M for the oxidation of phenylhydrazine were obtained as 11.0 s ^-1 and 0.30 mM, respectively. The generation of superoxides during the oxidation of phenylhydrazine by tyrosinase was monitored by nitroblue tetrazolium (NBT) assay. In the phenylhydrazine-tyrosinase reaction, 1 mol O₂ was required for the production of 1 mol phenol and 1/6 mol superoxide. The decomposition of superoxide by superoxide dismutase enhanced the rate constant of the oxidation of phenylhydrazine. Phenol formed in the oxidation of phenylhydrazine by tyrosinase was further oxidized by tyrosinase to an o-quinone, after the oxidation of phenylhydrazine by tyrosinase was almost completed.

Original language	English
Pages (from-to)	2420-2429
Number of pages	10
Journal	Applied Biochemistry and Biotechnology
Volume	169
Issue number	8
DOIs	https://doi.org/10.1007/s12010-013-0165-7
State	Published - 1 Apr 2013

Keywords

Phenol
Phenylhydrazine
Superoxide
Tyrosinase

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title = "The oxidation of phenylhydrazine by tyrosinase",

abstract = "Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25°C). The values of kcat and K M for the oxidation of phenylhydrazine were obtained as 11.0 s -1 and 0.30 mM, respectively. The generation of superoxides during the oxidation of phenylhydrazine by tyrosinase was monitored by nitroblue tetrazolium (NBT) assay. In the phenylhydrazine-tyrosinase reaction, 1 mol O2 was required for the production of 1 mol phenol and 1/6 mol superoxide. The decomposition of superoxide by superoxide dismutase enhanced the rate constant of the oxidation of phenylhydrazine. Phenol formed in the oxidation of phenylhydrazine by tyrosinase was further oxidized by tyrosinase to an o-quinone, after the oxidation of phenylhydrazine by tyrosinase was almost completed.",

keywords = "Phenol, Phenylhydrazine, Superoxide, Tyrosinase",

author = "Sung, {Yi Ming} and Gayam, {Srivardhan Reddy} and Shu-Pao Wu",

year = "2013",

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doi = "10.1007/s12010-013-0165-7",

language = "English",

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T1 - The oxidation of phenylhydrazine by tyrosinase

AU - Sung, Yi Ming

AU - Gayam, Srivardhan Reddy

AU - Wu, Shu-Pao

PY - 2013/4/1

Y1 - 2013/4/1

N2 - Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25°C). The values of kcat and K M for the oxidation of phenylhydrazine were obtained as 11.0 s -1 and 0.30 mM, respectively. The generation of superoxides during the oxidation of phenylhydrazine by tyrosinase was monitored by nitroblue tetrazolium (NBT) assay. In the phenylhydrazine-tyrosinase reaction, 1 mol O2 was required for the production of 1 mol phenol and 1/6 mol superoxide. The decomposition of superoxide by superoxide dismutase enhanced the rate constant of the oxidation of phenylhydrazine. Phenol formed in the oxidation of phenylhydrazine by tyrosinase was further oxidized by tyrosinase to an o-quinone, after the oxidation of phenylhydrazine by tyrosinase was almost completed.

AB - Tyrosinase was found to catalyze the oxidation of phenylhydrazine to phenol in a reaction that did not resemble those typically performed by tyrosinase. The kinetics of this reaction was investigated by measuring the initial velocity of the formation of phenol (25°C). The values of kcat and K M for the oxidation of phenylhydrazine were obtained as 11.0 s -1 and 0.30 mM, respectively. The generation of superoxides during the oxidation of phenylhydrazine by tyrosinase was monitored by nitroblue tetrazolium (NBT) assay. In the phenylhydrazine-tyrosinase reaction, 1 mol O2 was required for the production of 1 mol phenol and 1/6 mol superoxide. The decomposition of superoxide by superoxide dismutase enhanced the rate constant of the oxidation of phenylhydrazine. Phenol formed in the oxidation of phenylhydrazine by tyrosinase was further oxidized by tyrosinase to an o-quinone, after the oxidation of phenylhydrazine by tyrosinase was almost completed.

KW - Phenol

KW - Phenylhydrazine

KW - Superoxide

KW - Tyrosinase

UR - http://www.scopus.com/inward/record.url?scp=84883815062&partnerID=8YFLogxK

U2 - 10.1007/s12010-013-0165-7

DO - 10.1007/s12010-013-0165-7

M3 - Article

C2 - 23456281

AN - SCOPUS:84883815062

VL - 169

SP - 2420

EP - 2429

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

SN - 0273-2289

IS - 8

ER -

The oxidation of phenylhydrazine by tyrosinase

Abstract

Keywords

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