Ammonia monooxygenase: a work in progress

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Authors: Thomas C. Arndt, Alexander L. Laughlin, Kyle M. Lancaster
Cited by: 2
References: 184

Abstract

OH, the structure and genetic underpinnings of this chemical behavior vary significantly. Further, there are many Cu-binding sites in AMO, and consequently there has been substantial discussion regarding the nature of the Cu site or sites responsible for substrate activation. Overall, AMO has largely eluded direct study because active protein has only recently been purified due to difficulties in cultivation of the native organism and recalcitrance of the protein to recombinant expression. This review is intended to serve as a primer to AMO, yielding the necessary context to understand its importance.

Fields of Study & Subjects

Bacterial Genetics and Biotechnology Metal-Catalyzed Oxygenation Mechanisms Metalloenzymes and iron-sulfur proteins

Publication details

Journal / source
Chemical Science
Publisher
Royal Society of Chemistry (RSC)
Volume
17
Issue
18
Pages
8934–8958
Publication date
1 January 2026
Language
EN