Jack Silver, Golzar al-Jaff, Jehad A. Taies, Michael T. Wilson, Daniel den Engelsen, George R. Fern, Terry G. Ireland
{"title":"CO与低自旋[Fe(II)(Por)L2]复合物结合的研究:有助于理解CO与血红蛋白和肌红蛋白的结合","authors":"Jack Silver, Golzar al-Jaff, Jehad A. Taies, Michael T. Wilson, Daniel den Engelsen, George R. Fern, Terry G. Ireland","doi":"10.1007/s00775-022-01969-w","DOIUrl":null,"url":null,"abstract":"<div><p>The visible and M?ssbauer spectra of [Fe(II)(Por)L<sub>2</sub>] and [Fe(II)(Por)L(CO)] complexes (where Por?=?protoporphyrin IX (PPIX) or tetra(<i>p</i>-sulfophenyl)porphyrin (TPPS) and L?=?an aliphatic or aromatic nitrogenous base) are reported and discussed. The results are compared to those of previously reported [Fe(II)(Por)L(CO)] complexes (where Por?=?PPIX, TPPS, PMXPP, TPP, OMTBP and OEP; L?=?a nitrogenous aromatic ligand) and HbCO (where Hb?=?haemoglobin) and MyCO (where My?=?myoglobin). A new approach, to extracting information from the M?ssbauer parameters has been developed by plotting those of the [Fe(II)(Por)L<sub>2</sub>] complexes against those of [Fe(II)(Por)L(CO)] complexes for the same ligands, has yielded a series of trend lines that show a significant dependence on both the nature of the porphyrin and also of the nitrogenous ligand. Different trend lines were found for aromatic nitrogenous ligands to aliphatic nitrogenous ligands showing that the porphyrins could donate different amounts of charge to the Fe(II) cations as the L ligand changed, and hence, they display electron sink properties. From the plots, it was shown that haemoglobin and myoglobin both bind CO very strongly compared to the model complexes studied herein. Using the reported structural and M?ssbauer data for the [Fe(II)(Por)L<sub>2</sub>] and [Fe(II)(Por)L(CO)] complexes, it proved possible and instructive to plot the M?ssbauer parameters against a number of the bond lengths around the Fe(II) cations. The interpretation of the resulting trend lines both supported and facilitated the extension of our findings enabling further understanding of the geometry of the bonding in CO haemoglobin and CO myoglobin.</p><h3>Graphical abstract</h3>\n <figure><div><div><div><picture><img></picture></div></div></div></figure>\n </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":null,"pages":null},"PeriodicalIF":2.7000,"publicationDate":"2022-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-022-01969-w.pdf","citationCount":"1","resultStr":"{\"title\":\"Studies on the binding of CO to low-spin [Fe(II)(Por)L2] complexes: an aid to understanding the binding of CO to haemoglobin and myoglobin\",\"authors\":\"Jack Silver, Golzar al-Jaff, Jehad A. Taies, Michael T. Wilson, Daniel den Engelsen, George R. Fern, Terry G. Ireland\",\"doi\":\"10.1007/s00775-022-01969-w\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The visible and M?ssbauer spectra of [Fe(II)(Por)L<sub>2</sub>] and [Fe(II)(Por)L(CO)] complexes (where Por?=?protoporphyrin IX (PPIX) or tetra(<i>p</i>-sulfophenyl)porphyrin (TPPS) and L?=?an aliphatic or aromatic nitrogenous base) are reported and discussed. The results are compared to those of previously reported [Fe(II)(Por)L(CO)] complexes (where Por?=?PPIX, TPPS, PMXPP, TPP, OMTBP and OEP; L?=?a nitrogenous aromatic ligand) and HbCO (where Hb?=?haemoglobin) and MyCO (where My?=?myoglobin). A new approach, to extracting information from the M?ssbauer parameters has been developed by plotting those of the [Fe(II)(Por)L<sub>2</sub>] complexes against those of [Fe(II)(Por)L(CO)] complexes for the same ligands, has yielded a series of trend lines that show a significant dependence on both the nature of the porphyrin and also of the nitrogenous ligand. Different trend lines were found for aromatic nitrogenous ligands to aliphatic nitrogenous ligands showing that the porphyrins could donate different amounts of charge to the Fe(II) cations as the L ligand changed, and hence, they display electron sink properties. From the plots, it was shown that haemoglobin and myoglobin both bind CO very strongly compared to the model complexes studied herein. Using the reported structural and M?ssbauer data for the [Fe(II)(Por)L<sub>2</sub>] and [Fe(II)(Por)L(CO)] complexes, it proved possible and instructive to plot the M?ssbauer parameters against a number of the bond lengths around the Fe(II) cations. The interpretation of the resulting trend lines both supported and facilitated the extension of our findings enabling further understanding of the geometry of the bonding in CO haemoglobin and CO myoglobin.</p><h3>Graphical abstract</h3>\\n <figure><div><div><div><picture><img></picture></div></div></div></figure>\\n </div>\",\"PeriodicalId\":603,\"journal\":{\"name\":\"JBIC Journal of Biological Inorganic Chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2022-12-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1007/s00775-022-01969-w.pdf\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"JBIC Journal of Biological Inorganic Chemistry\",\"FirstCategoryId\":\"1\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s00775-022-01969-w\",\"RegionNum\":3,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"JBIC Journal of Biological Inorganic Chemistry","FirstCategoryId":"1","ListUrlMain":"https://link.springer.com/article/10.1007/s00775-022-01969-w","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Studies on the binding of CO to low-spin [Fe(II)(Por)L2] complexes: an aid to understanding the binding of CO to haemoglobin and myoglobin
The visible and M?ssbauer spectra of [Fe(II)(Por)L2] and [Fe(II)(Por)L(CO)] complexes (where Por?=?protoporphyrin IX (PPIX) or tetra(p-sulfophenyl)porphyrin (TPPS) and L?=?an aliphatic or aromatic nitrogenous base) are reported and discussed. The results are compared to those of previously reported [Fe(II)(Por)L(CO)] complexes (where Por?=?PPIX, TPPS, PMXPP, TPP, OMTBP and OEP; L?=?a nitrogenous aromatic ligand) and HbCO (where Hb?=?haemoglobin) and MyCO (where My?=?myoglobin). A new approach, to extracting information from the M?ssbauer parameters has been developed by plotting those of the [Fe(II)(Por)L2] complexes against those of [Fe(II)(Por)L(CO)] complexes for the same ligands, has yielded a series of trend lines that show a significant dependence on both the nature of the porphyrin and also of the nitrogenous ligand. Different trend lines were found for aromatic nitrogenous ligands to aliphatic nitrogenous ligands showing that the porphyrins could donate different amounts of charge to the Fe(II) cations as the L ligand changed, and hence, they display electron sink properties. From the plots, it was shown that haemoglobin and myoglobin both bind CO very strongly compared to the model complexes studied herein. Using the reported structural and M?ssbauer data for the [Fe(II)(Por)L2] and [Fe(II)(Por)L(CO)] complexes, it proved possible and instructive to plot the M?ssbauer parameters against a number of the bond lengths around the Fe(II) cations. The interpretation of the resulting trend lines both supported and facilitated the extension of our findings enabling further understanding of the geometry of the bonding in CO haemoglobin and CO myoglobin.
期刊介绍:
Biological inorganic chemistry is a growing field of science that embraces the principles of biology and inorganic chemistry and impacts other fields ranging from medicine to the environment. JBIC (Journal of Biological Inorganic Chemistry) seeks to promote this field internationally. The Journal is primarily concerned with advances in understanding the role of metal ions within a biological matrix—be it a protein, DNA/RNA, or a cell, as well as appropriate model studies. Manuscripts describing high-quality original research on the above topics in English are invited for submission to this Journal. The Journal publishes original articles, minireviews, and commentaries on debated issues.