Metal Preferences and Metallation
The metal binding preferences of most metalloproteins do not match their metal requirements. Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with ∼25% acquiring preassembled metal cofactors. The remaining ∼70% are presumed to compete for metals from buffer...
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| Veröffentlicht in: | The Journal of biological chemistry 2014-10, Vol.289 (41), p.28095-28103 |
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| container_end_page | 28103 |
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| container_issue | 41 |
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| container_title | The Journal of biological chemistry |
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| creator | Foster, Andrew W. Osman, Deenah Robinson, Nigel J. |
| description | The metal binding preferences of most metalloproteins do not match their metal requirements. Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with ∼25% acquiring preassembled metal cofactors. The remaining ∼70% are presumed to compete for metals from buffered metal pools. Metallation is further aided by maintaining the relative concentrations of these pools as an inverse function of the stabilities of the respective metal complexes. For example, magnesium enzymes always prefer to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems. Therefore, the buffered concentration of zinc is held at least a million-fold below magnesium inside most cells. |
| doi_str_mv | 10.1074/jbc.R114.588145 |
| format | Article |
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Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with ∼25% acquiring preassembled metal cofactors. The remaining ∼70% are presumed to compete for metals from buffered metal pools. Metallation is further aided by maintaining the relative concentrations of these pools as an inverse function of the stabilities of the respective metal complexes. For example, magnesium enzymes always prefer to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems. 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Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with ∼25% acquiring preassembled metal cofactors. The remaining ∼70% are presumed to compete for metals from buffered metal pools. Metallation is further aided by maintaining the relative concentrations of these pools as an inverse function of the stabilities of the respective metal complexes. For example, magnesium enzymes always prefer to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems. Therefore, the buffered concentration of zinc is held at least a million-fold below magnesium inside most cells.</description><subject>Bacillus subtilis - chemistry</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biological Transport</subject><subject>Clostridium - chemistry</subject><subject>Clostridium - metabolism</subject><subject>Cyanobacteria - chemistry</subject><subject>Cyanobacteria - metabolism</subject><subject>Escherichia coli - chemistry</subject><subject>Escherichia coli - metabolism</subject><subject>Helicobacter pylori - chemistry</subject><subject>Helicobacter pylori - metabolism</subject><subject>Iron - chemistry</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Magnesium - chemistry</subject><subject>Magnesium - metabolism</subject><subject>Manganese - chemistry</subject><subject>Manganese - metabolism</subject><subject>Metalloproteins - chemistry</subject><subject>Metalloproteins - metabolism</subject><subject>Minireviews</subject><subject>Models, Molecular</subject><subject>Thermodynamics</subject><subject>Zinc - chemistry</subject><subject>Zinc - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1LAzEQxYMotlbP3qTevGybSTbZ7EWQ4hdUFFHwFpJsqinb3ZpsC_73Zt1a9CAYAoHJbx4z7yF0DHgEOEvHc21GjwDpiAkBKdtBfcCCJpTByy7qY0wgyQkTPXQQwhzHk-awj3qEAcec8D46vbONKocP3s6st5WxYaiqYvhVLVXj6uoQ7c1UGezR5h2g56vLp8lNMr2_vp1cTBPDCGkSyLIsz3JlMBEEUyW0IZoXRIPIhBamENTYgnMujKYYK2Apx4yyWWwqtM7oAJ13usuVXtjC2KrxqpRL7xbKf8haOfn7p3Jv8rVeyxRykvI0CpxtBHz9vrKhkQsXjI1rVLZeBQlcZPECZf9AiWCEC9GONe5Q4-sQok3biQDLNgMZM5BtBrLLIHac_Fxky3-bHoG8A2y0c-2sl8G41vvCeWsaWdTuT_FPXueUPQ</recordid><startdate>20141010</startdate><enddate>20141010</enddate><creator>Foster, Andrew W.</creator><creator>Osman, Deenah</creator><creator>Robinson, Nigel J.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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>7U7</scope><scope>C1K</scope><scope>5PM</scope></search><sort><creationdate>20141010</creationdate><title>Metal Preferences and Metallation</title><author>Foster, Andrew W. ; 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| subjects | Bacillus subtilis - chemistry Bacillus subtilis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biological Transport Clostridium - chemistry Clostridium - metabolism Cyanobacteria - chemistry Cyanobacteria - metabolism Escherichia coli - chemistry Escherichia coli - metabolism Helicobacter pylori - chemistry Helicobacter pylori - metabolism Iron - chemistry Iron - metabolism Kinetics Magnesium - chemistry Magnesium - metabolism Manganese - chemistry Manganese - metabolism Metalloproteins - chemistry Metalloproteins - metabolism Minireviews Models, Molecular Thermodynamics Zinc - chemistry Zinc - metabolism |
| title | Metal Preferences and Metallation |
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