Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea-Reference-Cited by-同舟云学术

Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea

Published:2009-01-01 Issue:1 Volume:155 Page:279-284
ISSN:1350-0872
Container-title:Microbiology
language:en
Short-container-title:

Author:

Gilch Stefan¹,Vogel Manja¹,Lorenz Matthias W.²,Meyer Ortwin¹,Schmidt Ingo¹

Affiliation:

1. Department of Microbiology, University of Bayreuth, 95447 Bayreuth, Germany

2. Department of Animal Ecology, University of Bayreuth, 95447 Bayreuth, Germany

Abstract

The ammonia monooxygenase (AMO) ofNitrosomonas europaeais a metalloenzyme that catalyses the oxidation of ammonia to hydroxylamine. We have identified histidine 191 of AmoA as the binding site for the oxidized mechanism-based inactivator acetylene. Binding of acetylene changed the molecular mass of His-191 from 155.15 to 197.2 Da (+42.05), providing evidence that acetylene was oxidized to ketene (CH2CO; 42.04 Da) which binds specifically to His-191. It must be assumed that His-191 is part of the acetylene-activating site in AMO or at least directly neighbours this site.

Publisher

Microbiology Society

Subject

Microbiology

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