Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria
| Autor: | Neil L. Kelleher, Amy C. Rosenzweig, Betelehem E. Lemma, Timothy L. Stemmler, Sharon Batelu, Brian M. Hoffman, Matthew O. Ross, Oriana S. Fisher, Paul M. Thomas, Grace E. Kenney, Victoria C. Sosnowski, Caroline J. DeHart, Soo Y. Ro |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Methane monooxygenase Copper protein Science Amino Acid Motifs Protein domain General Physics and Astronomy Ligands 010402 general chemistry 01 natural sciences Article General Biochemistry Genetics and Molecular Biology Methane 03 medical and health sciences Ammonia chemistry.chemical_compound Hydroxylamine Bacterial Proteins Protein Domains Homeostasis lcsh:Science Multidisciplinary biology Chemistry Betaproteobacteria General Chemistry Ammonia monooxygenase biology.organism_classification 0104 chemical sciences 030104 developmental biology Biochemistry 13. Climate action biology.protein lcsh:Q Protein Multimerization Oxidation-Reduction Copper Bacteria |
| Zdroj: | Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018) Nature Communications |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-018-06681-5 |
| Popis: | 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 CuA 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. Methane- and ammonia-oxidizing bacteria use the integral membrane, copper-dependent enzymes particulate methane monooxygenase (pMMO) and ammonia monooxygenase (AMO) to oxidize methane and ammonia. Here the authors structurally characterize the copper-binding protein PmoD, which contains an unusual CuA site and their genetic analyses strongly support a pMMO and AMO related function of PmoD. |
| Databáze: | OpenAIRE |
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