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Purification of hydroxylamine oxidase from Thiosphaera pantotropha
Author(s) -
Wehrfritz Josa-Marie,
Reilly Ann,
Spiro Stephen,
Richardson David J.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80739-h
Subject(s) - hydroxylamine , periplasmic space , nitrification , chemistry , biochemistry , oxidase test , denitrifying bacteria , denitrification , enzyme , organic chemistry , escherichia coli , nitrogen , gene
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.