{"title":"血红蛋白还原铁(III)络合物的光谱分析:可能的相互作用机制","authors":"John P. Harrington, Rodgers L. Hicks","doi":"10.1016/0020-711X(94)90133-3","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Hemoglobin is capable of electron transfer to Fe(III)-complexes of ATP, EDTA, NTA, and citrate leading to formation of reduced Fe(II) and its concurrent release from these chelating compounds as evident in the formation of a Fe(II)-Tris 2,2' bipyridine complex.</p></span></li><li><span>2.</span><span><p>2. Multi-component analysis of kinetic spectra in the visible region (700–500 nm) has permitted a determination of the effect of various chelating molecules bound to Fe(III), pH, the effects of ionic strength, temperature, and the molecular nature of the Fe(III)-complex on reaction rates.</p></span></li><li><span>3.</span><span><p>3. We have examined and compared the reactivities of normal adult hemoglobin A (α<sub>2</sub> β<sub>2</sub>) to reduce these Fe(III)-complexes and suggest possible mechanism(s) for the electron transfer process.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 9","pages":"Pages 1111-1117"},"PeriodicalIF":0.0000,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90133-3","citationCount":"8","resultStr":"{\"title\":\"Spectral analysis of Fe(III)-complex reduction by hemoglobin: Possible mechanisms of interaction\",\"authors\":\"John P. Harrington, Rodgers L. Hicks\",\"doi\":\"10.1016/0020-711X(94)90133-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. Hemoglobin is capable of electron transfer to Fe(III)-complexes of ATP, EDTA, NTA, and citrate leading to formation of reduced Fe(II) and its concurrent release from these chelating compounds as evident in the formation of a Fe(II)-Tris 2,2' bipyridine complex.</p></span></li><li><span>2.</span><span><p>2. Multi-component analysis of kinetic spectra in the visible region (700–500 nm) has permitted a determination of the effect of various chelating molecules bound to Fe(III), pH, the effects of ionic strength, temperature, and the molecular nature of the Fe(III)-complex on reaction rates.</p></span></li><li><span>3.</span><span><p>3. We have examined and compared the reactivities of normal adult hemoglobin A (α<sub>2</sub> β<sub>2</sub>) to reduce these Fe(III)-complexes and suggest possible mechanism(s) for the electron transfer process.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 9\",\"pages\":\"Pages 1111-1117\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90133-3\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94901333\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94901333","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Spectral analysis of Fe(III)-complex reduction by hemoglobin: Possible mechanisms of interaction
1.
1. Hemoglobin is capable of electron transfer to Fe(III)-complexes of ATP, EDTA, NTA, and citrate leading to formation of reduced Fe(II) and its concurrent release from these chelating compounds as evident in the formation of a Fe(II)-Tris 2,2' bipyridine complex.
2.
2. Multi-component analysis of kinetic spectra in the visible region (700–500 nm) has permitted a determination of the effect of various chelating molecules bound to Fe(III), pH, the effects of ionic strength, temperature, and the molecular nature of the Fe(III)-complex on reaction rates.
3.
3. We have examined and compared the reactivities of normal adult hemoglobin A (α2 β2) to reduce these Fe(III)-complexes and suggest possible mechanism(s) for the electron transfer process.
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