Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 88
Volume 88, Issue -, Pages 409-431Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-013118-111529
Keywords
methane; monooxygenase; oxygen activation; kinetics; crystallography; spectroscopy
Categories
Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R35GM118030] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM040466, R01 GM100943, R35 GM118030] Funding Source: Medline
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Aerobic life is possible because the molecular structure of oxygen (O-2) 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 O-2 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 O-2 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.
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