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从兼性嗜盐芽孢杆菌1-73中纯化和鉴定亚硝酸盐氧化酶,并特别关注过氧化氢酶。

Purification and characterization of nitrite-oxidizing enzyme from heterotrophic Bacillus badius 1-73, with special concern to catalase.

作者信息

Sakai K, Nisijima H, Ikenaga Y, Wakayama M, Moriguchi M

机构信息

Department of Applied Chemistry, Faculty of Engineering, Oita University, Japan.

出版信息

Biosci Biotechnol Biochem. 2000 Dec;64(12):2727-30. doi: 10.1271/bbb.64.2727.

DOI:10.1271/bbb.64.2727
PMID:11210148
Abstract

Nitrite-oxidizing enzyme I (NiOx I) was purified from a heterotrophic bacterium, Bacillus badius I-73. The enzyme was a homotetramer of a heme-containing peptide, and was similar to catalases from various sources in its N-terminal amino acid sequence. The purified enzyme also catalyzed H2O2 degradation. The nitrite oxidation reaction required ascorbic acid and oxygen. Successive H2O2 feeding could be substituted for ascorbic acid. These indicated that NiOx I is a catalase and nitrite was oxidized by a peroxidase-like reaction.

摘要

亚硝酸氧化酶I(NiOx I)是从异养细菌巴氏芽孢杆菌I-73中纯化得到的。该酶是一种含血红素肽的同四聚体,其N端氨基酸序列与来自不同来源的过氧化氢酶相似。纯化后的酶也催化过氧化氢的降解。亚硝酸氧化反应需要抗坏血酸和氧气。连续加入过氧化氢可以替代抗坏血酸。这些表明NiOx I是一种过氧化氢酶,并且亚硝酸通过类似过氧化物酶的反应被氧化。

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