PURIFICATION AND CHARACTERIZATION OF THE ALKENE MONOOXYGENASE FROM NOCARDIA-CORALLINA B-276
UNSPECIFIED. (1995) PURIFICATION AND CHARACTERIZATION OF THE ALKENE MONOOXYGENASE FROM NOCARDIA-CORALLINA B-276. BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 59 (5). pp. 853-859. ISSN 0916-8451Full text not available from this repository.
Alkene monooxygenase from the propene utilizer Nocardia corallina B-276 was separated into three components, and all components were purified to homogeneity and their properties were examined, The epoxidase, with a molecular mass of 95kDa, was considered to catalyze the oxidation of the substrate propene to propylene oxide, It consisted of 53- and 35-kDa subunits, which contained approximately 2-mol of non-heme iron per mole of protein. The reductase, molecular mass 40 kDa, was found to contain an FAD and an Fe-2 S-2 cluster, A third protein, which we have called the coupling protein, with a mass of 14 kDa, appears to function as a regulator of activity. The purified AMO system required NADH as an electron donor, and catalyzed alkene epoxidation only, Acetylene, a specific inhibitor for methane monooxygenase, did not inhibit the AMO activity.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
T Technology > TP Chemical technology
T Technology > TX Home economics
|Journal or Publication Title:||BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY|
|Publisher:||JAPAN SOC BIOSCI BIOTECHN AGROCHEM|
|Official Date:||May 1995|
|Number of Pages:||7|
|Page Range:||pp. 853-859|
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