Purification and characterization of nitrite-oxidizing enzyme from heterotrophic bacillus badius i-73, with special concern to catalase

Kenji Sakai; Hiroto Nisijima; Yoshihito Ikenaga; Mamoru Wakayama; Mitsuaki Moriguchi

doi:10.1271/bbb.64.2727

Purification and characterization of nitrite-oxidizing enzyme from heterotrophic bacillus badius i-73, with special concern to catalase

Kenji Sakai, Hiroto Nisijima, Yoshihito Ikenaga, Mamoru Wakayama, Mitsuaki Moriguchi

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

9 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2727-2730
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	64
Issue number	12
DOIs	https://doi.org/10.1271/bbb.64.2727
Publication status	Published - Jun 2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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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.",

author = "Kenji Sakai and Hiroto Nisijima and Yoshihito Ikenaga and Mamoru Wakayama and Mitsuaki Moriguchi",

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T1 - Purification and characterization of nitrite-oxidizing enzyme from heterotrophic bacillus badius i-73, with special concern to catalase

AU - Sakai, Kenji

AU - Nisijima, Hiroto

AU - Ikenaga, Yoshihito

AU - Wakayama, Mamoru

AU - Moriguchi, Mitsuaki

PY - 2000/6

Y1 - 2000/6

N2 - 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.

AB - 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.

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

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ER -

Purification and characterization of nitrite-oxidizing enzyme from heterotrophic bacillus badius i-73, with special concern to catalase

Abstract

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