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PURIFICATION AND CHARACTERIZATION OF THE ALKENE MONOOXYGENASE FROM NOCARDIA-CORALLINA B-276
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UNSPECIFIED (1995) PURIFICATION AND CHARACTERIZATION OF THE ALKENE MONOOXYGENASE FROM NOCARDIA-CORALLINA B-276. BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 59 (5). pp. 853-859. ISSN 0916-8451.
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Abstract
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 | ||||
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Subjects: | Q Science > QD Chemistry T Technology > TP Chemical technology T Technology > TX Home economics |
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Journal or Publication Title: | BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | ||||
Publisher: | JAPAN SOC BIOSCI BIOTECHN AGROCHEM | ||||
ISSN: | 0916-8451 | ||||
Official Date: | May 1995 | ||||
Dates: |
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Volume: | 59 | ||||
Number: | 5 | ||||
Number of Pages: | 7 | ||||
Page Range: | pp. 853-859 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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