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

Autor: Fisher OS; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Kenney GE; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Ross MO; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Ro SY; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Lemma BE; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Batelu S; Department of Pharmaceutical Sciences, Wayne State University, Detroit, 48201, MI, USA., Thomas PM; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Sosnowski VC; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., DeHart CJ; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Kelleher NL; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Stemmler TL; Department of Pharmaceutical Sciences, Wayne State University, Detroit, 48201, MI, USA., Hoffman BM; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA., Rosenzweig AC; Departments of Molecular Biosciences and Chemistry, Northwestern University, Evanston, 60208, IL, USA. amyr@northwestern.edu.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2018 Oct 15; Vol. 9 (1), pp. 4276. Date of Electronic Publication: 2018 Oct 15.
DOI: 10.1038/s41467-018-06681-5
Abstrakt: 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 A 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.
Databáze: MEDLINE
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