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X-Ray Absorption Fine-Structure Spectroscopy Studies of Fe Sites in Natural Human Neuromelanin and Synthetic Analogues
X-ray absorption fine-structure spectroscopy is used to study the local environment of the iron site in natural (human) neuromelanin extracted from substantia nigra tissue and in various synthetic neuromelanins. All the materials show Fe centered in a nearest neighbor sixfold (distorted) oxygen octa...
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| Published in: | Biophysical journal 1998-12, Vol.75 (6), p.3135-3142 |
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| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c462t-c60427392f93302243d43e4194fa72a46bd5adcc342e605da0fee0e3394190d63 |
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| cites | cdi_FETCH-LOGICAL-c462t-c60427392f93302243d43e4194fa72a46bd5adcc342e605da0fee0e3394190d63 |
| container_end_page | 3142 |
| container_issue | 6 |
| container_start_page | 3135 |
| container_title | Biophysical journal |
| container_volume | 75 |
| creator | Kropf, A.J. Bunker, B.A. Eisner, M. Moss, S.C. Zecca, L. Stroppolo, A. Crippa, P.R. |
| description | X-ray absorption fine-structure spectroscopy is used to study the local environment of the iron site in natural (human) neuromelanin extracted from substantia nigra tissue and in various synthetic neuromelanins. All the materials show Fe centered in a nearest neighbor sixfold (distorted) oxygen octahedron; the Fe-O distances, while slightly different in the natural and synthetic neuromelanin, are both ∼2.0
Å. Appreciable differences arise, however, in the second (and higher) coordination shells. In this case the synthetic melanin has the four planar oxygens bound to carbon rings with Fe-C distances of ∼2.82 and 4.13
Å; the human sample does not show the 2.82
Å link but instead indicates a double shell at approximately 3.45 and 3.78
Å. |
| doi_str_mv | 10.1016/S0006-3495(98)77755-0 |
| format | article |
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Å. Appreciable differences arise, however, in the second (and higher) coordination shells. In this case the synthetic melanin has the four planar oxygens bound to carbon rings with Fe-C distances of ∼2.82 and 4.13
Å; the human sample does not show the 2.82
Å link but instead indicates a double shell at approximately 3.45 and 3.78
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Å. Appreciable differences arise, however, in the second (and higher) coordination shells. In this case the synthetic melanin has the four planar oxygens bound to carbon rings with Fe-C distances of ∼2.82 and 4.13
Å; the human sample does not show the 2.82
Å link but instead indicates a double shell at approximately 3.45 and 3.78
Å.</description><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Carbon - chemistry</subject><subject>Fourier Analysis</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Iron - chemistry</subject><subject>Melanins - chemical synthesis</subject><subject>Melanins - chemistry</subject><subject>Oxygen - chemistry</subject><subject>Spectrum Analysis</subject><subject>Substantia Nigra - chemistry</subject><subject>X-Rays</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFkV-L1DAUxYso67j6ERb6JO5D9Tb_2rwow-K4wqJgFXwLmeR2N9I2NUkH5tub2RkGffIpCefce0_uryiuanhbQy3edQAgKsokfyPb66ZpOK_gSbGqOSMVQCueFquz5XnxIsZfADXhUF8UF7IlQlC2KnY_q296X6630Yc5OT-VGzdh1aWwmLQELLsZTQo-Gj_vyy4t1mEsfV9usuRSvrup_KKzVQ_l7TLq_MIl-BEHPWVJT7bs9lN6wORMuZ704O8XjC-LZ70eIr46nZfFj83H7ze31d3XT59v1neVYYKkyghgpKGS9JJSIIRRyyiyWrJeN0QzsbVcW2MoIyiAWw09IiClMnvACnpZvD_2nZftiNbglHJQNQc36rBXXjv1rzK5B3Xvd6omUsqW5wavTw2C_52DJzW6aHDIv0O_RNUANMABspEfjSYvKwbsz0NqUAdg6hGYOtBQslWPwNSh7urvhOeqE6GsfzjqmNe0cxhUNA4ng9aFTEZZ7_4z4Q8tSKek</recordid><startdate>19981201</startdate><enddate>19981201</enddate><creator>Kropf, A.J.</creator><creator>Bunker, B.A.</creator><creator>Eisner, M.</creator><creator>Moss, S.C.</creator><creator>Zecca, L.</creator><creator>Stroppolo, A.</creator><creator>Crippa, P.R.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19981201</creationdate><title>X-Ray Absorption Fine-Structure Spectroscopy Studies of Fe Sites in Natural Human Neuromelanin and Synthetic Analogues</title><author>Kropf, A.J. ; Bunker, B.A. ; Eisner, M. ; Moss, S.C. ; Zecca, L. ; Stroppolo, A. ; Crippa, P.R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-c60427392f93302243d43e4194fa72a46bd5adcc342e605da0fee0e3394190d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Carbon - chemistry</topic><topic>Fourier Analysis</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Iron - chemistry</topic><topic>Melanins - chemical synthesis</topic><topic>Melanins - chemistry</topic><topic>Oxygen - chemistry</topic><topic>Spectrum Analysis</topic><topic>Substantia Nigra - chemistry</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kropf, A.J.</creatorcontrib><creatorcontrib>Bunker, B.A.</creatorcontrib><creatorcontrib>Eisner, M.</creatorcontrib><creatorcontrib>Moss, S.C.</creatorcontrib><creatorcontrib>Zecca, L.</creatorcontrib><creatorcontrib>Stroppolo, A.</creatorcontrib><creatorcontrib>Crippa, P.R.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kropf, A.J.</au><au>Bunker, B.A.</au><au>Eisner, M.</au><au>Moss, S.C.</au><au>Zecca, L.</au><au>Stroppolo, A.</au><au>Crippa, P.R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>X-Ray Absorption Fine-Structure Spectroscopy Studies of Fe Sites in Natural Human Neuromelanin and Synthetic Analogues</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1998-12-01</date><risdate>1998</risdate><volume>75</volume><issue>6</issue><spage>3135</spage><epage>3142</epage><pages>3135-3142</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>X-ray absorption fine-structure spectroscopy is used to study the local environment of the iron site in natural (human) neuromelanin extracted from substantia nigra tissue and in various synthetic neuromelanins. All the materials show Fe centered in a nearest neighbor sixfold (distorted) oxygen octahedron; the Fe-O distances, while slightly different in the natural and synthetic neuromelanin, are both ∼2.0
Å. Appreciable differences arise, however, in the second (and higher) coordination shells. In this case the synthetic melanin has the four planar oxygens bound to carbon rings with Fe-C distances of ∼2.82 and 4.13
Å; the human sample does not show the 2.82
Å link but instead indicates a double shell at approximately 3.45 and 3.78
Å.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9826634</pmid><doi>10.1016/S0006-3495(98)77755-0</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 1998-12, Vol.75 (6), p.3135-3142 |
| issn | 0006-3495 1542-0086 |
| language | eng |
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| source | PubMed (Medline) |
| subjects | Biophysical Phenomena Biophysics Carbon - chemistry Fourier Analysis Humans In Vitro Techniques Iron - chemistry Melanins - chemical synthesis Melanins - chemistry Oxygen - chemistry Spectrum Analysis Substantia Nigra - chemistry X-Rays |
| title | X-Ray Absorption Fine-Structure Spectroscopy Studies of Fe Sites in Natural Human Neuromelanin and Synthetic Analogues |
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