Author
Listed:
- Oriana S. Fisher
(Northwestern University)
- Grace E. Kenney
(Northwestern University)
- Matthew O. Ross
(Northwestern University)
- Soo Y. Ro
(Northwestern University)
- Betelehem E. Lemma
(Northwestern University)
- Sharon Batelu
(Wayne State University)
- Paul M. Thomas
(Northwestern University)
- Victoria C. Sosnowski
(Northwestern University)
- Caroline J. DeHart
(Northwestern University)
- Neil L. Kelleher
(Northwestern University)
- Timothy L. Stemmler
(Wayne State University)
- Brian M. Hoffman
(Northwestern University)
- Amy C. Rosenzweig
(Northwestern University)
Abstract
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.
Suggested Citation
Oriana S. Fisher & Grace E. Kenney & Matthew O. Ross & Soo Y. Ro & Betelehem E. Lemma & Sharon Batelu & Paul M. Thomas & Victoria C. Sosnowski & Caroline J. DeHart & Neil L. Kelleher & Timothy L. Stem, 2018.
"Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria,"
Nature Communications, Nature, vol. 9(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06681-5
DOI: 10.1038/s41467-018-06681-5
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