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

Microbiology
Stefan GilchIngo Schmidt

Abstract

The ammonia monooxygenase (AMO) of Nitrosomonas europaea is 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.

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Citations

Nov 15, 2012·Proceedings of the National Academy of Sciences of the United States of America·Amy M Weeks, Michelle C Y Chang
May 21, 2009·Biological Chemistry·Stefan GilchIngo Schmidt
Mar 6, 2010·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Stefan GilchIngo Schmidt
Jun 26, 2012·Critical Reviews in Biochemistry and Molecular Biology·Megen A Culpepper, Amy C Rosenzweig
Jan 23, 2016·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Peter M H Kroneck
Jan 31, 2016·Applied and Environmental Microbiology·Kristen BennettMichael R Hyman
May 23, 2019·Angewandte Chemie·Sebastian Wendeborn
Feb 23, 2020·Applied and Environmental Microbiology·Chloë L WrightLaura E Lehtovirta-Morley
Oct 4, 2011·Nature·Boran KartalMarc Strous
Nov 24, 2016·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Matthew O Ross, Amy C Rosenzweig
Sep 4, 2020·Chembiochem : a European Journal of Chemical Biology·Rita Fuerst, Rolf Breinbauer
Sep 6, 2020·The Science of the Total Environment·Mario Corrochano-MonsalveBeñat Artetxe

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