Oxalate-dependent reductive activity of manganese peroxidase from Phanerochaete chrysosporium.
Oxalate-dependent reductive activity of manganese peroxidase from Phanerochaete chrysosporium.
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黄孢原毛平革菌锰过氧化物酶的草酸盐依赖性还原活性。
DOI:
10.1006/abbi.1994.1446
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发表时间:
1994
影响因子:
3.9
通讯作者:
Aust,SD
中科院分区:
文献类型:
--
作者:
Khindaria,A;Grover,TA;Aust,SD
The mechanism of oxalate-dependent reductive activity of a manganese-dependent peroxidase (MnP) fromPhanerochaete chrysosporiumwas investigated. Ferric iron reduction was demonstrated in reaction mixtures containing Mn-peroxidase, Mn2+, oxalate, H2O2, ferric chloride, and 1,10-phenanthroline. Only catalytic amounts of H2O2were required. Oxygen consumption was also observed in reaction mixtures containing Mn-peroxidase, Mn2+, oxalate, and H2O2and was inhibited by the addition of ferric iron. Electron spin resonance studies, using the spin traps 5,5-dimethyl-1-pyrroline-N-oxide and α-4-pyridyl-1-oxide-N-t-butylnitrone were used to obtain evidence for the production of the formate radical (CO.2−) and superoxide (O.2−) in a reaction mixture containing Mn2+, oxalate and H2O2. It was concluded that both CO.2−(anaerobic conditions) and O.2−(aerobic conditions) could reduce ferric iron. The dismutation of some O.2−would produce H2O2to provide a constant supply of H2O2.