{"title":"红细胞铜蛋白,也称为超氧化物歧化酶,是一种氢醌氧化酶,对丝裂霉素C产生耐药性","authors":"P. Penketh","doi":"10.20455/ros.2022.c803","DOIUrl":null,"url":null,"abstract":"The enzymatic function of superoxide dismutase (SOD) is proposed to be as a ubiquinol oxidase. The SOD activity of this protein is likely a consequence of the necessary dismutation of superoxide (O2˙ˉ), generated as an enzyme-bound intermediate during its normal activity. The relatively low specificity of this enzyme for hydroquinones allowed it to oxidize a wide range of hydroquinone substrates. The general hydroquinone oxidase activity of this enzyme would thus enable it to behave as a mammalian analogue to bacterial mitomycin C resistance protein (MCRA). This would account for its elevated activity in cells expressing resistance against mitomycin C, porfiromycin, and related analogues, since superoxide itself is relatively nontoxic.","PeriodicalId":91793,"journal":{"name":"Reactive oxygen species (Apex, N.C.)","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Erythrocuprein, also Known as Superoxide Dismutase, Is a Hydroquinone Oxidase, and Imparts Resistance to Mitomycin C\",\"authors\":\"P. Penketh\",\"doi\":\"10.20455/ros.2022.c803\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The enzymatic function of superoxide dismutase (SOD) is proposed to be as a ubiquinol oxidase. The SOD activity of this protein is likely a consequence of the necessary dismutation of superoxide (O2˙ˉ), generated as an enzyme-bound intermediate during its normal activity. The relatively low specificity of this enzyme for hydroquinones allowed it to oxidize a wide range of hydroquinone substrates. The general hydroquinone oxidase activity of this enzyme would thus enable it to behave as a mammalian analogue to bacterial mitomycin C resistance protein (MCRA). This would account for its elevated activity in cells expressing resistance against mitomycin C, porfiromycin, and related analogues, since superoxide itself is relatively nontoxic.\",\"PeriodicalId\":91793,\"journal\":{\"name\":\"Reactive oxygen species (Apex, N.C.)\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-05-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Reactive oxygen species (Apex, N.C.)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.20455/ros.2022.c803\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Reactive oxygen species (Apex, N.C.)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.20455/ros.2022.c803","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Erythrocuprein, also Known as Superoxide Dismutase, Is a Hydroquinone Oxidase, and Imparts Resistance to Mitomycin C
The enzymatic function of superoxide dismutase (SOD) is proposed to be as a ubiquinol oxidase. The SOD activity of this protein is likely a consequence of the necessary dismutation of superoxide (O2˙ˉ), generated as an enzyme-bound intermediate during its normal activity. The relatively low specificity of this enzyme for hydroquinones allowed it to oxidize a wide range of hydroquinone substrates. The general hydroquinone oxidase activity of this enzyme would thus enable it to behave as a mammalian analogue to bacterial mitomycin C resistance protein (MCRA). This would account for its elevated activity in cells expressing resistance against mitomycin C, porfiromycin, and related analogues, since superoxide itself is relatively nontoxic.