CHEMICAL MODIFICATION OF THE HYDROXYLASE OF SOLUBLE METHANE MONOOXYGENASE GIVES ONE FORM OF THE PROTEIN WITH SIGNIFICANTLY INCREASED THERMOSTABILITY AND ANOTHER THAT FUNCTIONS WELL IN ORGANIC-SOLVENTS
UNSPECIFIED. (1994) CHEMICAL MODIFICATION OF THE HYDROXYLASE OF SOLUBLE METHANE MONOOXYGENASE GIVES ONE FORM OF THE PROTEIN WITH SIGNIFICANTLY INCREASED THERMOSTABILITY AND ANOTHER THAT FUNCTIONS WELL IN ORGANIC-SOLVENTS. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1201 (1). pp. 76-84. ISSN 0304-4165Full text not available from this repository.
Proteolysis of the hydroxylase component of soluble methane monooxygenase (MMO) with trypsin yielded a protein which retained 50% activity in a standard MMO assay. In an H2O2-driven assay, in which H2O2 replaced two of the protein components, NADH and O-2 used in the standard assay, the proteolysed hydroxylase retained full activity for ethane, propane and propene, but had a 2-3-fold increase with methane as substrate. Several crosslinking reagents have been tested for their ability to stabilise the proteolysed form of the hydroxylase. Using polyoxyethylene bis(imidazolyl carbonyl) (M(r) 3350) as the crosslinking agent, increased thermostability of the hydroxylase was observed. Activated methoxypolyethylene glycol(M(r) 5000) was used to modify the hydroxylase which was now soluble in organic solvents as well as water and could be activated by H2O2. The glycol-modified hydroxylase functioned well in organic solvents in the catalysis of propene oxidation.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS|
|Publisher:||ELSEVIER SCIENCE BV|
|Official Date:||28 September 1994|
|Number of Pages:||9|
|Page Range:||pp. 76-84|
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