van Pée K H, Lingens F
J Bacteriol. 1985 Mar;161(3):1171-5. doi: 10.1128/jb.161.3.1171-1175.1985.
A Bromoperoxidase has been isolated and purified from Pseudomonas aureofaciens ATCC 15926 mutant strain ACN. The purified enzyme was homogeneous as determined by polyacrylamide gel electrophoresis and ultracentrifugation. This bromoperoxidase can utilize bromide ions in the presence of hydrogen peroxide and a halogen acceptor for the catalytic formation of carbon-halogen bonds. The homogeneous enzyme also has peroxidase and catalase activity. Based on the results from gel filtration and ultracentrifugation, the molecular weight of this procaryotic bromoperoxidase is 155,000 to 158,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows a single band having the mobility of a 77,000-molecular-weight species. We thus conclude that this bromoperoxidase exists in solution as a dimeric species. The heme prosthetic group of bromoperoxidase is ferriprotoporphyrin IX. The spectral properties of the native and reduced enzyme are reported. This bromoperoxidase is the first halogenating enzyme purified from procaryotic sources.
已从金黄色假单胞菌ATCC 15926突变株ACN中分离并纯化出一种溴过氧化物酶。通过聚丙烯酰胺凝胶电泳和超速离心测定，纯化后的酶具有均一性。这种溴过氧化物酶在过氧化氢和卤素受体存在的情况下，能够利用溴离子催化形成碳-卤键。该均一酶还具有过氧化物酶和过氧化氢酶活性。根据凝胶过滤和超速离心结果，这种原核溴过氧化物酶的分子量为155,000至158,000。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示出一条具有77,000分子量物质迁移率的单一谱带。因此，我们得出结论，这种溴过氧化物酶在溶液中以二聚体形式存在。溴过氧化物酶的血红素辅基是高铁原卟啉IX。报告了天然酶和还原酶的光谱特性。这种溴过氧化物酶是首个从原核生物来源纯化得到的卤化酶。
