Abstract:
:Aerobic life is possible because the molecular structure of oxygen (O2) makes direct reaction with most organic materials at ambient temperatures an exceptionally slow process. Of course, these reactions are inherently very favorable, and they occur rapidly with the release of a great deal of energy at high temperature. Nature has been able to tap this sequestered reservoir of energy with great spatial and temporal selectivity at ambient temperatures through the evolution of oxidase and oxygenase enzymes. One mechanism used by these enzymes for O2 activation has been studied in detail for the soluble form of the enzyme methane monooxygenase. These studies have revealed the step-by-step process of O2 activation and insertion into the ultimately stable C-H bond of methane. Additionally, an elegant regulatory mechanism has been defined that enlists size selection and quantum tunneling to allow methane oxidation to occur specifically in the presence of more easily oxidized substrates.
journal_name
Annu Rev Biochemjournal_title
Annual review of biochemistryauthors
Banerjee R,Jones JC,Lipscomb JDdoi
10.1146/annurev-biochem-013118-111529subject
Has Abstractpub_date
2019-06-20 00:00:00pages
409-431eissn
0066-4154issn
1545-4509journal_volume
88pub_type
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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journal_title:Annual review of biochemistry
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