Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3903
Title: Synthesis, crystal structures and protease activity of amino acid Schiff base iron(III) complexes
Authors: Begum, Mohammed S Ameerunisha
Nethaji, Sounik Saha, Munirathinam
Chakravarty, Akhil R
Keywords: Bioinorganic chemistry
Protein binding
Protein cleavage
Crystal structure Amino acids
Iron
Issue Date: Apr-2009
Publisher: CSIR
Series/Report no.: Int. Cl. <sup>8</sup> C07F15/04
Abstract: Iron(III) complexes, (NHEt<sub>3</sub>)[Fe(III)(sal-met)<sub>2</sub>] and (NHEt<sub>3</sub>)[Fe(III)(sal-phe)<sub>2</sub>], of amino acid Schiff base ligands, viz., <i>N</i>-salicylidene-L-methionine and <i>N</i>-salicylidene-L-phenylalanine, have been prepared and their binding to bovine serum albumin (BSA) and photo-induced BSA cleavage activity have been investigated. The complexes are structurally characterized by single crystal X-ray crystallography. The crystal structures of the discrete mononuclear monoanionic complexes show FeN<sub>2</sub>O<sub>4</sub> octahedral coordination geometry in which the tridentate dianionic amino acid Schiff base ligand binds through phenolate and carboxylate oxygen and imine nitrogen atoms. The imine nitrogen atoms are <i style="">trans</i> to each other. The Fe-O and Fe-N bond distances range between 1.9 and 2.1 Å. The sal-met complex has two pendant thiomethyl groups. The high-spin iron(III) complexes (<meta http-equiv="Content-Type" content="text/html; charset=utf-8"><meta name="ProgId" content="Word.Document"><meta name="Generator" content="Microsoft Word 11"><meta name="Originator" content="Microsoft Word 11"><link rel="File-List" href="file:///C:%5CDOCUME%7E1%5CLovely%5CLOCALS%7E1%5CTemp%5Cmsohtml1%5C01%5Cclip_filelist.xml"><!--[if gte mso 9]><xml> <w:WordDocument> <w:View>Normal</w:View> <w:Zoom>0</w:Zoom> <w:PunctuationKerning/> <w:ValidateAgainstSchemas/> <w:SaveIfXMLInvalid>false</w:SaveIfXMLInvalid> <w:IgnoreMixedContent>false</w:IgnoreMixedContent> <w:AlwaysShowPlaceholderText>false</w:AlwaysShowPlaceholderText> <w:Compatibility> <w:BreakWrappedTables/> <w:SnapToGridInCell/> <w:WrapTextWithPunct/> <w:UseAsianBreakRules/> <w:DontGrowAutofit/> </w:Compatibility> <w:BrowserLevel>MicrosoftInternetExplorer4</w:BrowserLevel> </w:WordDocument> </xml><![endif]--><!--[if gte mso 9]><xml> <w:LatentStyles DefLockedState="false" LatentStyleCount="156"> </w:LatentStyles> </xml><![endif]--><style> <!-- /* Font Definitions */ @font-face {font-family:Mangal; panose-1:0 0 4 0 0 0 0 0 0 0; mso-font-charset:0; mso-generic-font-family:auto; mso-font-pitch:variable; mso-font-signature:32771 0 0 0 1 0;} /* Style Definitions */ p.MsoNormal, li.MsoNormal, div.MsoNormal {mso-style-parent:""; margin:0in; margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:12.0pt; font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal; mso-bidi-language:HI;} @page Section1 {size:8.5in 11.0in; margin:1.0in 1.25in 1.0in 1.25in; mso-header-margin:.5in; mso-footer-margin:.5in; mso-paper-source:0;} div.Section1 {page:Section1;} --> </style><!--[if gte mso 10]> <style> /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-parent:""; mso-padding-alt:0in 5.4pt 0in 5.4pt; mso-para-margin:0in; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Times New Roman"; mso-ansi-language:#0400; mso-fareast-language:#0400; mso-bidi-language:#0400;} </style> <![endif]--><span style="font-size: 12pt;" times="" new="" roman="" ;="" color:="" black;="">μ</span><sub>eff</sub> ~ 5.9 <meta http-equiv="Content-Type" content="text/html; charset=utf-8"><meta name="ProgId" content="Word.Document"><meta name="Generator" content="Microsoft Word 11"><meta name="Originator" content="Microsoft Word 11"><link rel="File-List" href="file:///C:%5CDOCUME%7E1%5CLovely%5CLOCALS%7E1%5CTemp%5Cmsohtml1%5C01%5Cclip_filelist.xml"><!--[if gte mso 9]><xml> <w:WordDocument> <w:View>Normal</w:View> <w:Zoom>0</w:Zoom> <w:PunctuationKerning/> <w:ValidateAgainstSchemas/> <w:SaveIfXMLInvalid>false</w:SaveIfXMLInvalid> <w:IgnoreMixedContent>false</w:IgnoreMixedContent> <w:AlwaysShowPlaceholderText>false</w:AlwaysShowPlaceholderText> <w:Compatibility> <w:BreakWrappedTables/> <w:SnapToGridInCell/> <w:WrapTextWithPunct/> <w:UseAsianBreakRules/> <w:DontGrowAutofit/> </w:Compatibility> <w:BrowserLevel>MicrosoftInternetExplorer4</w:BrowserLevel> </w:WordDocument> </xml><![endif]--><!--[if gte mso 9]><xml> <w:LatentStyles DefLockedState="false" LatentStyleCount="156"> </w:LatentStyles> </xml><![endif]--><style> <!-- /* Font Definitions */ @font-face {font-family:Mangal; panose-1:0 0 4 0 0 0 0 0 0 0; mso-font-charset:0; mso-generic-font-family:auto; mso-font-pitch:variable; mso-font-signature:32771 0 0 0 1 0;} /* Style Definitions */ p.MsoNormal, li.MsoNormal, div.MsoNormal {mso-style-parent:""; margin:0in; margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:12.0pt; font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:Mangal; mso-bidi-language:HI;} @page Section1 {size:8.5in 11.0in; margin:1.0in 1.25in 1.0in 1.25in; mso-header-margin:.5in; mso-footer-margin:.5in; mso-paper-source:0;} div.Section1 {page:Section1;} --> </style><!--[if gte mso 10]> <style> /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-parent:""; mso-padding-alt:0in 5.4pt 0in 5.4pt; mso-para-margin:0in; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Times New Roman"; mso-ansi-language:#0400; mso-fareast-language:#0400; mso-bidi-language:#0400;} </style> <![endif]--><span style="font-size: 12pt;" times="" new="" roman="" ;="" color:="" black;="">μ</span><sub>B</sub>) exhibit quasi-reversible Fe(III)/Fe(II) redox process near -0.6 V vs. SCE in water. These complexes display a visible electronic band near 480 nm in tris-HCl buffer assignable to the phenolate-to-iron(III) charge transfer transition. The water soluble complexes bind to BSA giving binding constant values of ~10<sup>5</sup> <i>M</i><sup>-1</sup>. The complexes show non-specific oxidative cleavage of BSA protein on photo-irradiation with UV-A light of 365 nm.
Description: 473-479
URI: http://hdl.handle.net/123456789/3903
ISSN: 0376-4710
Appears in Collections:IJC-A Vol.48A(04) [April 2009]

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