A Putative Fe2+-Bound Persulfenate Intermediate in Cysteine Dioxygenase
The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 Å resolution crystal structure of the Fe2+-dependent enzyme cysteine dioxygenase (CDO) containing this put...
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| Veröffentlicht in: | Biochemistry 2008-11, Vol.47 (44), p.11390-11392 |
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| container_title | Biochemistry |
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| creator | Simmons, Chad R Krishnamoorthy, Kalyanaraman Granett, Spencer L Schuller, David J Dominy, John E Begley, Tadhg P Stipanuk, Martha H Karplus, P. Andrew |
| description | The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 Å resolution crystal structure of the Fe2+-dependent enzyme cysteine dioxygenase (CDO) containing this putative intermediate trapped in its active site pocket. The complex raises the possibility that, distinct from known dioxygenases and proposed CDO mechanisms, the Fe-proximal oxygen atom may be involved in the primary oxidation event yielding a unique three-membered Fe−S−O cyclic intermediate. A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product. |
| doi_str_mv | 10.1021/bi801546n |
| format | Article |
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A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi801546n</identifier><identifier>PMID: 18847220</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; ATOMS ; BASIC BIOLOGICAL SCIENCES ; Catalytic Domain ; CRYSTAL STRUCTURE ; Crystallography, X-Ray ; CYSTEINE ; Cysteine - analogs & derivatives ; Cysteine - chemistry ; Cysteine - metabolism ; Cysteine Dioxygenase - chemistry ; Cysteine Dioxygenase - metabolism ; ENVIRONMENT ; ENZYMES ; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE ; In Vitro Techniques ; Iron - metabolism ; ISOMERIZATION ; Liver - enzymology ; MATERIALS SCIENCE ; Models, Molecular ; national synchrotron light source ; OXIDATION ; Oxidation-Reduction ; OXYGEN ; Protein Conformation ; Rats ; RESOLUTION ; Sulfenic Acids - chemistry ; Sulfenic Acids - metabolism</subject><ispartof>Biochemistry, 2008-11, Vol.47 (44), p.11390-11392</ispartof><rights>Copyright © 2008 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi801546n$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi801546n$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,780,784,885,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18847220$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/979986$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Simmons, Chad R</creatorcontrib><creatorcontrib>Krishnamoorthy, Kalyanaraman</creatorcontrib><creatorcontrib>Granett, Spencer L</creatorcontrib><creatorcontrib>Schuller, David J</creatorcontrib><creatorcontrib>Dominy, John E</creatorcontrib><creatorcontrib>Begley, Tadhg P</creatorcontrib><creatorcontrib>Stipanuk, Martha H</creatorcontrib><creatorcontrib>Karplus, P. Andrew</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><title>A Putative Fe2+-Bound Persulfenate Intermediate in Cysteine Dioxygenase</title><title>Biochemistry</title><addtitle>Biochemistry</addtitle><description>The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 Å resolution crystal structure of the Fe2+-dependent enzyme cysteine dioxygenase (CDO) containing this putative intermediate trapped in its active site pocket. The complex raises the possibility that, distinct from known dioxygenases and proposed CDO mechanisms, the Fe-proximal oxygen atom may be involved in the primary oxidation event yielding a unique three-membered Fe−S−O cyclic intermediate. A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product.</description><subject>Animals</subject><subject>ATOMS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Catalytic Domain</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>CYSTEINE</subject><subject>Cysteine - analogs & derivatives</subject><subject>Cysteine - chemistry</subject><subject>Cysteine - metabolism</subject><subject>Cysteine Dioxygenase - chemistry</subject><subject>Cysteine Dioxygenase - metabolism</subject><subject>ENVIRONMENT</subject><subject>ENZYMES</subject><subject>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</subject><subject>In Vitro Techniques</subject><subject>Iron - metabolism</subject><subject>ISOMERIZATION</subject><subject>Liver - enzymology</subject><subject>MATERIALS SCIENCE</subject><subject>Models, Molecular</subject><subject>national synchrotron light source</subject><subject>OXIDATION</subject><subject>Oxidation-Reduction</subject><subject>OXYGEN</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>RESOLUTION</subject><subject>Sulfenic Acids - chemistry</subject><subject>Sulfenic Acids - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkU1PGzEQhq2KqgTaQ_9AtRzaC1pqe3f9cakEARIQUiORnkeOMwumG5uuvYj8exyFRnCyRvNo_Mw7hHxl9IRRzn4unKKsqYX_QEas4bSstW72yIhSKkquBd0nBzE-5LKmsv5E9plSteScjsjktJgNyST3hMUl8uPyLAx-Wcywj0PXojcJiyufsF_h0m0K54vxOiZ0HotzF57XdxmK-Jl8bE0X8cvre0j-XF7Mx9Py5vfkanx6U5pK6VRy21hplm3bKsWo0lK3KPhSqUoIwXlla45yocTCsJay2jDNhBZ5G8GyOlbVIfm1nfs4LLKSRZ9608Fj71amX0MwDt53vLuHu_AEXOSVlcwDjrYDQkwOonUJ7b0N3qNNkH20Epn58fpJH_4NGBOsXLTYdcZjGCIILZkSbGPz7a3NTuN_vhkot4DLkT3v-qb_C0JWsoH57BbOJ7fX07PpHKaZ_77ljY3wEIbe5zCBUdjcGXZ3rl4AROKWNw</recordid><startdate>20081104</startdate><enddate>20081104</enddate><creator>Simmons, Chad R</creator><creator>Krishnamoorthy, Kalyanaraman</creator><creator>Granett, Spencer L</creator><creator>Schuller, David J</creator><creator>Dominy, John E</creator><creator>Begley, Tadhg P</creator><creator>Stipanuk, Martha H</creator><creator>Karplus, P. Andrew</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20081104</creationdate><title>A Putative Fe2+-Bound Persulfenate Intermediate in Cysteine Dioxygenase</title><author>Simmons, Chad R ; Krishnamoorthy, Kalyanaraman ; Granett, Spencer L ; Schuller, David J ; Dominy, John E ; Begley, Tadhg P ; Stipanuk, Martha H ; Karplus, P. 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Andrew</creatorcontrib><creatorcontrib>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simmons, Chad R</au><au>Krishnamoorthy, Kalyanaraman</au><au>Granett, Spencer L</au><au>Schuller, David J</au><au>Dominy, John E</au><au>Begley, Tadhg P</au><au>Stipanuk, Martha H</au><au>Karplus, P. Andrew</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Putative Fe2+-Bound Persulfenate Intermediate in Cysteine Dioxygenase</atitle><jtitle>Biochemistry</jtitle><addtitle>Biochemistry</addtitle><date>2008-11-04</date><risdate>2008</risdate><volume>47</volume><issue>44</issue><spage>11390</spage><epage>11392</epage><pages>11390-11392</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 Å resolution crystal structure of the Fe2+-dependent enzyme cysteine dioxygenase (CDO) containing this putative intermediate trapped in its active site pocket. The complex raises the possibility that, distinct from known dioxygenases and proposed CDO mechanisms, the Fe-proximal oxygen atom may be involved in the primary oxidation event yielding a unique three-membered Fe−S−O cyclic intermediate. A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>18847220</pmid><doi>10.1021/bi801546n</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemistry, 2008-11, Vol.47 (44), p.11390-11392 |
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| source | ACS_美国化学学会期刊（与NSTL共建）; MEDLINE |
| subjects | Animals ATOMS BASIC BIOLOGICAL SCIENCES Catalytic Domain CRYSTAL STRUCTURE Crystallography, X-Ray CYSTEINE Cysteine - analogs & derivatives Cysteine - chemistry Cysteine - metabolism Cysteine Dioxygenase - chemistry Cysteine Dioxygenase - metabolism ENVIRONMENT ENZYMES GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE In Vitro Techniques Iron - metabolism ISOMERIZATION Liver - enzymology MATERIALS SCIENCE Models, Molecular national synchrotron light source OXIDATION Oxidation-Reduction OXYGEN Protein Conformation Rats RESOLUTION Sulfenic Acids - chemistry Sulfenic Acids - metabolism |
| title | A Putative Fe2+-Bound Persulfenate Intermediate in Cysteine Dioxygenase |
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