Purification of hydroxylamine oxidase from Thiosphaera pantotropha

FEBS Letters

Spiro, Stephen¹  Reilly, Ann¹  Richardson, David J.¹  Wehrfritz, Josa-Marie¹ 

[1]School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK

关键词: Nitrification;    Denitrification;    Hydroxylamine oxidase;    Thiosphaera pantotropha;   

DOI  :  10.1016/0014-5793(93)80739-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thiosphaera pantotropha, a Gram-negative heterotrophic nitrifying bacterium, expresses a soluble 20 kDa monomeric periplasmic hydroxylamine oxidase that differs markedly from the hydroxylamine oxidase found in autotrophic bacteria. This enzyme can use the periplasmic redox proteins, cytochrome C ₅₅₁ and pseudoazurin as electron acceptors, both of which can also donate electrons to denitrification enzymes. A model of electron transfer is proposed, that suggests a coupling of nitrification to denitrification and provides a mechanism by which nitrification can play a role in dissipating reductant.

【 授权许可】

Unknown