Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 40, Issue 7, Pages 475-483Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar700052v
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Funding
- NIGMS NIH HHS [R01 GM040466-18, R37 GM024689, R01 GM040466-16, R01 GM024689, R01 GM024689-28, R37 GM024689-26, R01 GM024689-27, R01 GM040466, GM24689, R01 GM040466-17, GM40466] Funding Source: Medline
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Intermediates in the reaction cycle of an oxygenase are usually very informative with respect to the chemical mechanism of O-2 activation and insertion. However, detection of these intermediates is often complicated by their short lifetime and the regulatory mechanism of the enzyme designed to ensure specificity. Here, the methods used to detect the intermediates in an extradiol dioxygenase, a Rieske cis-dihydrodiol dioxygenase, and soluble methane monooxygenase are discussed. The methods include the use of alternative, chromophoric substrates, mutagenesis of active site catalytic residues, forced changes in substrate binding order, control of reaction rates using regulatory proteins, and initialization of catalysis in crystallo.
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