Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase
Lysine 2,3-aminomutase (KAM) belongs to a class of enzymes that use FeS clusters and S-adenosyl-l-methionine to initiate radical-dependent chemistry. Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenos...
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| Veröffentlicht in: | Biochemistry (Easton) 2000-12, Vol.39 (51), p.15668-15673 |
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| container_issue | 51 |
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| container_title | Biochemistry (Easton) |
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| creator | Cosper, Nathaniel J Booker, Squire J Ruzicka, Frank Frey, Perry A Scott, Robert A |
| description | Lysine 2,3-aminomutase (KAM) belongs to a class of enzymes that use FeS clusters and S-adenosyl-l-methionine to initiate radical-dependent chemistry. Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenosyl-l-selenomethionine, reveals that the cofactor is cleaved only in the presence of dithionite and the substrate analogue trans-4,5-dehydrolysine. A new Fourier transform peak at 2.7 Å, assigned as a Se−Fe interaction, appears concomitant with this cleavage. This is the first demonstration of a direct interaction of S-adenosyl-l-methionine, or its cleavage products, with the FeS cluster in this class of enzymes. |
| doi_str_mv | 10.1021/bi0022184 |
| format | Article |
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Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenosyl-l-selenomethionine, reveals that the cofactor is cleaved only in the presence of dithionite and the substrate analogue trans-4,5-dehydrolysine. A new Fourier transform peak at 2.7 Å, assigned as a Se−Fe interaction, appears concomitant with this cleavage. 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Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenosyl-l-selenomethionine, reveals that the cofactor is cleaved only in the presence of dithionite and the substrate analogue trans-4,5-dehydrolysine. A new Fourier transform peak at 2.7 Å, assigned as a Se−Fe interaction, appears concomitant with this cleavage. This is the first demonstration of a direct interaction of S-adenosyl-l-methionine, or its cleavage products, with the FeS cluster in this class of enzymes.</description><subject>Deoxyadenosines - chemistry</subject><subject>Dithionite - chemistry</subject><subject>Fourier Analysis</subject><subject>Free Radicals - metabolism</subject><subject>Hydrolysis</subject><subject>Intramolecular Transferases - chemistry</subject><subject>Intramolecular Transferases - metabolism</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Iron-Sulfur Proteins - metabolism</subject><subject>Lysine - analogs & derivatives</subject><subject>Lysine - chemistry</subject><subject>Selenomethionine - analogs & derivatives</subject><subject>Selenomethionine - chemistry</subject><subject>Spectrum Analysis</subject><subject>Substrate Specificity</subject><subject>X-Rays</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkF1LwzAUhoMoOqcX_gHJjYJgNR9t2l7K1DkYKE6vQ5qeQGabatKK-_dmbMwbLw6Hw_vwHngQOqPkhhJGbytLCGO0SPfQiGaMJGlZZvtoRAgRCSsFOULHISzjmZI8PURHlFLGi5KO0OLeetA9foQFnjRD6MHjmfvumm9owfXYOjwFB171tnO4M1jhV1VbrZp1NF8F6wCza57ctdZ17dCrACfowKgmwOl2j9H748Pb5CmZP09nk7t5onha9klBgWeKGyOEritVMWN0UYmapXmcTIm8qjRnHLiqNKGsjiTjQhsqcgqp4WN0uen99N3XAKGXrQ0amkY56IYgc5YWBc-zCF5tQO27EDwY-eltq_xKUiLXBuXOYGTPt6VD1UL9R26VRSDZADbK-tnlyn9Ikcdv8u1lIRdT9ppNSCHvI3-x4ZUOctkN3kUn_zz-BdCEhTU</recordid><startdate>20001226</startdate><enddate>20001226</enddate><creator>Cosper, Nathaniel J</creator><creator>Booker, Squire J</creator><creator>Ruzicka, Frank</creator><creator>Frey, Perry A</creator><creator>Scott, Robert A</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>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20001226</creationdate><title>Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase</title><author>Cosper, Nathaniel J ; Booker, Squire J ; Ruzicka, Frank ; Frey, Perry A ; Scott, Robert A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-81e35a3ff66cdbab2ffc8b6d247d245a67bbc323e3abc012dff6236cf1671e4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Deoxyadenosines - chemistry</topic><topic>Dithionite - chemistry</topic><topic>Fourier Analysis</topic><topic>Free Radicals - metabolism</topic><topic>Hydrolysis</topic><topic>Intramolecular Transferases - chemistry</topic><topic>Intramolecular Transferases - metabolism</topic><topic>Iron-Sulfur Proteins - chemistry</topic><topic>Iron-Sulfur Proteins - metabolism</topic><topic>Lysine - analogs & derivatives</topic><topic>Lysine - chemistry</topic><topic>Selenomethionine - analogs & derivatives</topic><topic>Selenomethionine - chemistry</topic><topic>Spectrum Analysis</topic><topic>Substrate Specificity</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cosper, Nathaniel J</creatorcontrib><creatorcontrib>Booker, Squire J</creatorcontrib><creatorcontrib>Ruzicka, Frank</creatorcontrib><creatorcontrib>Frey, Perry A</creatorcontrib><creatorcontrib>Scott, Robert A</creatorcontrib><collection>Istex</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><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cosper, Nathaniel J</au><au>Booker, Squire J</au><au>Ruzicka, Frank</au><au>Frey, Perry A</au><au>Scott, Robert A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2000-12-26</date><risdate>2000</risdate><volume>39</volume><issue>51</issue><spage>15668</spage><epage>15673</epage><pages>15668-15673</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Lysine 2,3-aminomutase (KAM) belongs to a class of enzymes that use FeS clusters and S-adenosyl-l-methionine to initiate radical-dependent chemistry. 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| ispartof | Biochemistry (Easton), 2000-12, Vol.39 (51), p.15668-15673 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Deoxyadenosines - chemistry Dithionite - chemistry Fourier Analysis Free Radicals - metabolism Hydrolysis Intramolecular Transferases - chemistry Intramolecular Transferases - metabolism Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - metabolism Lysine - analogs & derivatives Lysine - chemistry Selenomethionine - analogs & derivatives Selenomethionine - chemistry Spectrum Analysis Substrate Specificity X-Rays |
| title | Direct FeS Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase |
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