The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity

被引：101

作者：

Forte, E

Urbani, A

Saraste, M

Sarti, P

Brunori, M

Giuffrè, A

机构：

[1] Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy

[2] Univ Roma La Sapienza, CNR, Ctr Mol Biol, I-00185 Rome, Italy

[3] European Mol Biol Lab, Heidelberg, Germany

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 2001年 / 268卷 / 24期

关键词：

respiration; evolution; denitrifying bacteria; spectroscopy;

D O I：

10.1046/j.0014-2956.2001.02597.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cytochrome cbb(3) is an isoenzyme in the family of cytochrome c oxidases. This protein purified from Pseudomonas stutzeri displays a cyanide-sensitive nitric oxide reductase activity (V-max=100 +/-9 mol NO.mol cbb(3)(-1).min(-1) and K-m=12 +/-2.5 mum), which is lost upon denaturation. This enzyme is only partially reduced by ascorbate, and readily re-oxidized by NO under anaerobic conditions at a rate consistent with the turnover number for NO consumption. As shown by transient spectroscopy experiments and singular value decomposition (SVD) analysis, these results suggest that the cbb(3)-type cytochromes, sharing structural features with bacterial nitric oxide reductases, are the enzymes retaining the highest NO reductase activity within the heme-copper oxidase superfamily.

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收藏

页码：6486 / 6490

页数：5

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