Interaction of the mechanism-based inactivator acetylene with ammonia monooxygenase of Nitrosomonas europaea
0301 basic medicine
0303 health sciences
Binding Sites
Acetylene
Molecular Sequence Data
Nitrosomonas europaea
Gene Expression Regulation, Bacterial
Ethylenes
Ketones
03 medical and health sciences
Histidine
Amino Acid Sequence
Carbon Radioisotopes
Oxidoreductases
Peptides
Oxidation-Reduction
DOI:
10.1099/mic.0.023721-0
Publication Date:
2008-12-31T23:06:09Z
AUTHORS (5)
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.
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