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• W2110586503 abstract "ABSTRACT In a previous study (M. Sasaki, J. Maki, K. Oshiman, Y. Matsumura, and T. Tsuchido, Biodegradation 16: 449-459, 2005), the cytochrome P450 monooxygenase system was shown to be involved in bisphenol A (BPA) degradation by Sphingomonas sp. strain AO1. In the present investigation, we purified the components of this monooxygenase, cytochrome P450 (P450 bisd ), ferredoxin (Fd bisd ), and ferredoxin reductase (Red bisd ). We demonstrated that P450 bisd and Fd bisd are homodimeric proteins with molecular masses of 102.3 and 19.1 kDa, respectively, by gel filtration chromatography analysis. Spectroscopic analysis of Fd bisd revealed the presence of a putidaredoxin-type [2Fe-2S] cluster. P450 bisd , in the presence of Fd bisd , Red bisd , and NADH, was able to convert BPA. The K m and k cat values for BPA degradation were 85 ± 4.7 μM and 3.9 ± 0.04 min −1 , respectively. NADPH, spinach ferredoxin, and spinach ferredoxin reductase resulted in weak monooxygenase activity. These results indicated that the electron transport system of P450 bisd might exhibit strict specificity. Two BPA degradation products of the P450 bisd system were detected by high-performance liquid chromatography analysis and were thought to be 1,2-bis(4-hydroxyphenyl)-2-propanol and 2,2-bis(4-hydroxyphenyl)-1-propanol based on mass spectrometry-mass spectrometry analysis. This is the first report demonstrating that the cytochrome P450 monooxygenase system in bacteria is involved in BPA degradation." @default.
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• W2110586503 date "2005-12-01" @default.
• W2110586503 modified "2023-10-17" @default.
• W2110586503 title "Purification of Cytochrome P450 and Ferredoxin, Involved in Bisphenol A Degradation, from <i>Sphingomonas</i> sp. Strain AO1" @default.
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• W2110586503 doi "https://doi.org/10.1128/aem.71.12.8024-8030.2005" @default.
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