Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-06681-5
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Funding
- Department of Energy [DE-SC0016284]
- National Institutes of Health [GM118035, GM111097, DK068139, R01AT009143, F32GM119191]
- American Heart Association [14PRE20460104]
- DOE Office of Science [DE-AC02-06CH11356]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Institute of General Medical Sciences
- NASA Ames Research Center [NNA06CB93G]
- National Resource for Translational and Developmental Proteomics under NIH [P41 GM108569]
- NCI CCSG [P30 CA060553]
- [P41GM103393]
- NATIONAL CANCER INSTITUTE [P30CA060553] Funding Source: NIH RePORTER
- National Center for Complementary & Integrative Health [R01AT009143] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK068139] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM111097, P41GM103393, T32GM008382, P41GM108569, F32GM119191, R35GM118035] Funding Source: NIH RePORTER
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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 copperdependent 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.
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