Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria

Methane-oxidizing microbes catalyze the oxidation of the greenhouse gas methane using the copper-dependent enzyme particulate methane monooxygenase (pMMO). Isolated pMMO exhibits lower activity than whole cells, however, suggesting that additional components may be required. A pMMO homolog, ammonia...

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Bibliographic Details
Published in:	Nature communications 2018-10, Vol.9 (1), p.4276-12, Article 4276
Main Authors:	Fisher, Oriana S, Kenney, Grace E, Ross, Matthew O, Ro, Soo Y, Lemma, Betelehem E, Batelu, Sharon, Thomas, Paul M, Sosnowski, Victoria C, DeHart, Caroline J, Kelleher, Neil L, Stemmler, Timothy L, Hoffman, Brian M, Rosenzweig, Amy C
Format:	Article
Language:	eng
Subjects:	Amino Acid Motifs Ammonia Ammonia - metabolism Ammonia monooxygenase Ammonia-oxidizing bacteria Bacteria Bacterial Proteins - chemistry Bacterial Proteins - metabolism BASIC BIOLOGICAL SCIENCES Betaproteobacteria - metabolism Carbon cycle Copper Copper - metabolism Genetic analysis Greenhouse effect Greenhouse gases Homeostasis Homology Hydroxylamine Ligands Methane Methane - metabolism Methane monooxygenase Nitrous oxide Operons Oxidation Oxidation-Reduction Protein Domains Protein Multimerization Proteins
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Summary:	Methane-oxidizing microbes catalyze the oxidation of the greenhouse gas methane using the copper-dependent enzyme particulate methane monooxygenase (pMMO). Isolated pMMO exhibits lower activity than whole cells, however, suggesting that additional components may be required. A pMMO homolog, ammonia monooxygenase (AMO), converts ammonia to hydroxylamine in ammonia-oxidizing bacteria (AOB) which produce another potent greenhouse gas, nitrous oxide. Here we show that PmoD, a protein encoded within many pmo operons that is homologous to the AmoD proteins encoded within AOB amo operons, forms a copper center that exhibits the features of a well-defined Cu site using a previously unobserved ligand set derived from a cupredoxin homodimer. PmoD is critical for copper-dependent growth on methane, and genetic analyses strongly support a role directly related to pMMO and AMO. These findings identify a copper-binding protein that may represent a missing link in the function of enzymes critical to the global carbon and nitrogen cycles.
ISSN:	2041-1723 2041-1723