{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T14:04:03Z","timestamp":1792073043493,"version":"4.4.0"},"reference-count":49,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2005,12,1]],"date-time":"2005-12-01T00:00:00Z","timestamp":1133395200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2005,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    In a previous study (M. Sasaki, J. Maki, K. Oshiman, Y. Matsumura, and T. Tsuchido, Biodegradation\n                    <jats:bold>16:<\/jats:bold>\n                    449-459, 2005), the cytochrome P450 monooxygenase system was shown to be involved in bisphenol A (BPA) degradation by\n                    <jats:italic>Sphingomonas<\/jats:italic>\n                    sp. strain AO1. In the present investigation, we purified the components of this monooxygenase, cytochrome P450 (P450\n                    <jats:sub>bisd<\/jats:sub>\n                    ), ferredoxin (Fd\n                    <jats:sub>bisd<\/jats:sub>\n                    ), and ferredoxin reductase (Red\n                    <jats:sub>bisd<\/jats:sub>\n                    ). We demonstrated that P450\n                    <jats:sub>bisd<\/jats:sub>\n                    and Fd\n                    <jats:sub>bisd<\/jats:sub>\n                    are homodimeric proteins with molecular masses of 102.3 and 19.1 kDa, respectively, by gel filtration chromatography analysis. Spectroscopic analysis of Fd\n                    <jats:sub>bisd<\/jats:sub>\n                    revealed the presence of a putidaredoxin-type [2Fe-2S] cluster. P450\n                    <jats:sub>bisd<\/jats:sub>\n                    , in the presence of Fd\n                    <jats:sub>bisd<\/jats:sub>\n                    , Red\n                    <jats:sub>bisd<\/jats:sub>\n                    , and NADH, was able to convert BPA. The\n                    <jats:italic>\n                      K\n                      <jats:sub>m<\/jats:sub>\n                    <\/jats:italic>\n                    and\n                    <jats:italic>k<\/jats:italic>\n                    <jats:sub>cat<\/jats:sub>\n                    values for BPA degradation were 85 \u00b1 4.7 \u03bcM and 3.9 \u00b1 0.04 min\n                    <jats:sup>\u22121<\/jats:sup>\n                    , respectively. NADPH, spinach ferredoxin, and spinach ferredoxin reductase resulted in weak monooxygenase activity. These results indicated that the electron transport system of P450\n                    <jats:sub>bisd<\/jats:sub>\n                    might exhibit strict specificity. Two BPA degradation products of the P450\n                    <jats:sub>bisd<\/jats:sub>\n                    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.\n                  <\/jats:p>","DOI":"10.1128\/aem.71.12.8024-8030.2005","type":"journal-article","created":{"date-parts":[[2005,12,6]],"date-time":"2005-12-06T06:07:48Z","timestamp":1133849268000},"page":"8024-8030","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":92,"title":["Purification of Cytochrome P450 and Ferredoxin, Involved in Bisphenol A Degradation, from\n                    <i>Sphingomonas<\/i>\n                    sp. Strain AO1"],"prefix":"10.1128","volume":"71","author":[{"given":"Miho","family":"Sasaki","sequence":"first","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ayako","family":"Akahira","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ko-ichi","family":"Oshiman","sequence":"additional","affiliation":[{"name":"Tsukuba Research Institute, Sumitomo Forestry Co., Ltd., 3-2 Midorigahara, Tsukuba 300-2646, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tetsuaki","family":"Tsuchido","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering"},{"name":"High Technology Research Center, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka 564-8680, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshinobu","family":"Matsumura","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Faculty of Engineering"},{"name":"High Technology Research Center, Kansai University, 3-3-35 Yamate-cho, Suita, Osaka 564-8680, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(78)52018-1"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1997.00833.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)50589-5"},{"key":"e_1_3_2_5_2","unstructured":"Colborn T. 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