Methane is a prevalent greenhouse gas that contributes to global warming. While synthetically it is difficult to chemically convert methane to less environmentally harmful substances, methanotrophic bacteria have developed an efficient way to metabolize methane. In the first step of the process, methanotrophs use a copper dependent enzyme complex called particulate methane monooxygenase (pMMO) to convert methane to methanol, but precisely how this occurs biochemically and how pMMO may be regulated are not well understood. The primary goal of this proposal is to characterize a protein called pmoD that is also likely involved in methane conversion and may somehow regulate pMMO. In one component of this work the phenotype of pmoD will be studied using a pmoD knockout strain. A second aspect of the work will focus on structural, biochemical, and spectroscopic characterization of pmoD.
The third aim addresses the function of pmoD by determining whether it can interact with other proteins involved in copper metabolism and methane conversion and whether it can regulate these processes. Together, this combination of in'vivo studies, structural characterization, and biochemical analysis is expected to provide a comprehensive description of pmoD and its roles in methane metabolism and copper regulation. The insights gained from these studies have the potential to greatly enhance the current understanding of biological methane oxidation. Biochemical analysis is expected to provide a comprehensive description of pmoD and its roles in methane metabolism and copper regulation. The insights gained from these studies have the potential to greatly enhance the current understanding of biological methane oxidation.

Public Health Relevance

Global levels of methane emissions have been increasing, and as a greenhouse gas, methane is a major contributor to global warming. Methanotrophic bacteria can efficiently convert this greenhouse gas to methanol. The process by which this occurs is not fully understood; therefore the proposed research will characterize a bacterial membrane protein called pmoD to test the hypothesis that it regulates the molecular machinery the bacteria use to carry out this process.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
3F32GM119191-01S1
Application #
9313692
Study Section
Program Officer
Barski, Oleg
Project Start
2016-07-01
Project End
2019-06-30
Budget Start
2016-07-01
Budget End
2017-06-30
Support Year
1
Fiscal Year
2017
Total Cost
$1,400
Indirect Cost
Name
Northwestern University at Chicago
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
160079455
City
Evanston
State
IL
Country
United States
Zip Code
60201
Fisher, Oriana S; Kenney, Grace E; Ross, Matthew O et al. (2018) Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nat Commun 9:4276