page_title: Stephen J. Lippard
section_title: Methane monooxygenases
hierarchical_section_title: Stephen J. Lippard / Research / Methane monooxygenases
caption_attribution_description: Particulate methane monooxygenase from the methanotroph Methylococcus capsulatus. Protein image from OPM database
context_page_description: Stephen James Lippard is the Arthur Amos Noyes Emeritus Professor of Chemistry at the Massachusetts Institute of Technology. He is considered one of the founders of bioinorganic chemistry, studying the interactions of nonliving substances such as metals with biological systems.
  He is also considered a founder of metalloneurochemistry, the study of metal ions and their effects in the brain and nervous system. He has done pioneering work in understanding protein structure and synthesis, the enzymatic functions of methane monooxygenase, and the mechanisms of cisplatin anticancer drugs. His work has applications for the treatment of cancer, for bioremediation of the environment, and for the development of synthetic methanol-based fuels.
context_section_description: Members of the Lippard laboratory studying macromolecular crystallography have explored the structure,  mechanisms and activity of bacterial multicomponent monooxygenases.
  Methane monooxygenases are enzymes that occur in bacteria called methanotrophs.
  The primary function of this enzyme is the hydroxylation of methane to methanol as the first step in methane metabolism.
  Amy Rosenzweig determined the protein x-ray structure of the soluble form of methane monooxygenase (MMO) as Lippard's graduate student. Lippard has used X-ray diffraction and a variety of other methods to study such compounds, greatly expanding our understanding of their structure and function. MMO is vital to Earth's carbon cycle, and knowledge of its structure may help to develop clean technologies for methanol-based fuels. Methane monoxygenases may also be useful for bioremediation.
caption: Particulate methane monooxygenase
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