Cytochrome a 3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase
The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm -1 , respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a 3...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1984-07, Vol.225 (4659), p.329-331 |
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| container_issue | 4659 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Argade, P. V. Ching, Y. C. Rousseau, D. L. |
| description | The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm
-1
, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a
3
is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a
3
is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions. |
| doi_str_mv | 10.1126/science.6330890 |
| format | Article |
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-1
, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a
3
is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a
3
is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.6330890</identifier><language>eng</language><ispartof>Science (American Association for the Advancement of Science), 1984-07, Vol.225 (4659), p.329-331</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c860-18c1c64cd0d70d1c897e4183f22c7a88a80519e5c97d0557cb00a680d674e9b93</citedby><cites>FETCH-LOGICAL-c860-18c1c64cd0d70d1c897e4183f22c7a88a80519e5c97d0557cb00a680d674e9b93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2884,2885,27924,27925</link.rule.ids></links><search><creatorcontrib>Argade, P. V.</creatorcontrib><creatorcontrib>Ching, Y. C.</creatorcontrib><creatorcontrib>Rousseau, D. L.</creatorcontrib><title>Cytochrome a 3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase</title><title>Science (American Association for the Advancement of Science)</title><description>The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm
-1
, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a
3
is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a
3
is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions.</description><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNpNkD1PwzAURS0EEqFlZvUfcPscx18jBChIRR3aPXKeHRFEY2QnEv33FJGB6Ur36tzhEHLHYcV5qdYZ-zBgWCkhwFi4IAUHK5ktQVySAkAoZkDLa3KT8wfAebOiII_1aYz4nuIxUEcF3Y9pwnFKgfYDrV1q40Df4hC_ex_YQ5wGT_8Ru3PtcliSq8595nA754Icnp8O9Qvb7jav9f2WoVHAuEGOqkIPXoPnaKwOFTeiK0vUzhhnQHIbJFrtQUqNLYBTBrzSVbCtFQuy_rvFFHNOoWu-Un906dRwaH4dNLODZnYgfgBFn1BQ</recordid><startdate>19840720</startdate><enddate>19840720</enddate><creator>Argade, P. V.</creator><creator>Ching, Y. C.</creator><creator>Rousseau, D. L.</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19840720</creationdate><title>Cytochrome a 3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase</title><author>Argade, P. V. ; Ching, Y. C. ; Rousseau, D. L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c860-18c1c64cd0d70d1c897e4183f22c7a88a80519e5c97d0557cb00a680d674e9b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Argade, P. V.</creatorcontrib><creatorcontrib>Ching, Y. C.</creatorcontrib><creatorcontrib>Rousseau, D. L.</creatorcontrib><collection>CrossRef</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Argade, P. V.</au><au>Ching, Y. C.</au><au>Rousseau, D. L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome a 3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><date>1984-07-20</date><risdate>1984</risdate><volume>225</volume><issue>4659</issue><spage>329</spage><epage>331</epage><pages>329-331</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm
-1
, respectively. The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a
3
is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five- and six-coordinate cytochrome a
3
is strained; and that the carbon monoxide and the proximal histidine each have characteristic, well-defined orientations in all molecules. These data can account for the binding affinities of carbon monoxide and dioxygen under physiological conditions.</abstract><doi>10.1126/science.6330890</doi><tpages>3</tpages></addata></record> |
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| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1984-07, Vol.225 (4659), p.329-331 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_crossref_primary_10_1126_science_6330890 |
| source | JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| title | Cytochrome a 3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase |
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