Steric Control of CO Binding in a Totally Synthetic Heme Protein Model
A family of totally synthetic models for the carbon monoxide adducts of heme proteins has been synthesized and applied to the elucidation of the role of steric effects in the relative detoxification of carbon monoxide. The complexes are designed such that a sheltered void of controllable dimensions...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1981-10, Vol.78 (10), p.5919-5923 |
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| container_issue | 10 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 78 |
| creator | Busch, Daryle H. Zimmer, L. Lawrence Grzybowski, Joseph J. Olszanski, Dennis J. Jackels, Susan C. Callahan, Robert C. Christoph, Gary G. |
| description | A family of totally synthetic models for the carbon monoxide adducts of heme proteins has been synthesized and applied to the elucidation of the role of steric effects in the relative detoxification of carbon monoxide. The complexes are designed such that a sheltered void of controllable dimensions encompasses the CO binding site. Systematic variations in the available space for the iron-bound CO produce a wide range of equilibrium binding constants (KCO). An x-ray structure determination of a CO adduct complex having a crowded CO site reveals that the Fe--C$\equiv $O linkage is bent, and further, the distortion involves both displacement of the Fe--C vector from the normal to the N4plane and bending of the Fe--C--O angle. |
| doi_str_mv | 10.1073/pnas.78.10.5919 |
| format | Article |
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An x-ray structure determination of a CO adduct complex having a crowded CO site reveals that the Fe--C$\equiv $O linkage is bent, and further, the distortion involves both displacement of the Fe--C vector from the normal to the N4plane and bending of the Fe--C--O angle.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.78.10.5919</identifier><identifier>PMID: 16593093</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adducts ; Atoms ; Bending ; Carbon monoxide ; Crystal structure ; Hemeproteins ; Isomers ; Ligands ; Nitrogen ; Physical Sciences: Chemistry ; Porphyrins</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1981-10, Vol.78 (10), p.5919-5923</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c463t-4872a9f1583551fda617361f1e75adacfa4f5f27f2443fbb913c8a44404a6fc43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/78/10.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/10973$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/10973$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,27929,27930,53796,53798,58022,58255</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16593093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Busch, Daryle H.</creatorcontrib><creatorcontrib>Zimmer, L. 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An x-ray structure determination of a CO adduct complex having a crowded CO site reveals that the Fe--C$\equiv $O linkage is bent, and further, the distortion involves both displacement of the Fe--C vector from the normal to the N4plane and bending of the Fe--C--O angle.</description><subject>Adducts</subject><subject>Atoms</subject><subject>Bending</subject><subject>Carbon monoxide</subject><subject>Crystal structure</subject><subject>Hemeproteins</subject><subject>Isomers</subject><subject>Ligands</subject><subject>Nitrogen</subject><subject>Physical Sciences: Chemistry</subject><subject>Porphyrins</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNp9kDFPwzAQhS0EglKYkRiQN6YUO7bjeGCACChSUZEKs-UmNgS5cbEdRP89iVqgLEyn033v7t0D4ASjEUacXCwbFUY875oRE1jsgAFGAicZFWgXDBBKeZLTlB6AwxDeEEKC5WgfHOCMCYIEGYDbWdS-LmHhmuidhc7AYgqv66aqmxdYN1DBJxeVtSs4WzXxVccOHuuFho_eRd0BD67S9gjsGWWDPt7UIXi-vXkqxslkendfXE2SkmYkJjTnqRIGs5wwhk2lMsxJhg3WnKlKlUZRw0zKTUopMfO5wKTMFaUUUZWZkpIhuFzvXbbzha5K3blWVi59vVB-JZ2q5d9JU7_KF_chCc1FZ2EIzjd6795bHaJc1KHU1qpGuzZITghDlKf9pYs1WXoXgtfm5whGss9e9tlLnvd9n32nONv29stvwt4CeuX3-M-G838BaVpro_6MHXm6Jt9CdH7Lmug--AK3WKEP</recordid><startdate>19811001</startdate><enddate>19811001</enddate><creator>Busch, Daryle H.</creator><creator>Zimmer, L. 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Lawrence</creatorcontrib><creatorcontrib>Grzybowski, Joseph J.</creatorcontrib><creatorcontrib>Olszanski, Dennis J.</creatorcontrib><creatorcontrib>Jackels, Susan C.</creatorcontrib><creatorcontrib>Callahan, Robert C.</creatorcontrib><creatorcontrib>Christoph, Gary G.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Busch, Daryle H.</au><au>Zimmer, L. 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Systematic variations in the available space for the iron-bound CO produce a wide range of equilibrium binding constants (KCO). An x-ray structure determination of a CO adduct complex having a crowded CO site reveals that the Fe--C$\equiv $O linkage is bent, and further, the distortion involves both displacement of the Fe--C vector from the normal to the N4plane and bending of the Fe--C--O angle.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>16593093</pmid><doi>10.1073/pnas.78.10.5919</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1981-10, Vol.78 (10), p.5919-5923 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_78_10_5919 |
| source | Full-Text Journals in Chemistry (Open access); PubMed Central; Alma/SFX Local Collection; JSTOR |
| subjects | Adducts Atoms Bending Carbon monoxide Crystal structure Hemeproteins Isomers Ligands Nitrogen Physical Sciences: Chemistry Porphyrins |
| title | Steric Control of CO Binding in a Totally Synthetic Heme Protein Model |
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