The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.
Three iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]<sub>H</sub> component of the catalytic H-cluster of FeFe hydrogenase. The radical <em>S</em>-adenosyl-<span style="font-variant: small-caps;">l</span>-methionin...
| Egile Nagusiak: | , , , , , , , , , |
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| Formatua: | Journal article |
| Hizkuntza: | English |
| Argitaratua: |
American Association for the Advancement of Science
2014
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| _version_ | 1826299274682433536 |
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| author | Kuchenreuther, J Myers, W Suess, D Stich, T Pelmenschikov, V Shiigi, SA Cramer, S Swartz, JR Britt, R George, S |
| author_facet | Kuchenreuther, J Myers, W Suess, D Stich, T Pelmenschikov, V Shiigi, SA Cramer, S Swartz, JR Britt, R George, S |
| author_sort | Kuchenreuther, J |
| collection | OXFORD |
| description | Three iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]<sub>H</sub> component of the catalytic H-cluster of FeFe hydrogenase. The radical <em>S</em>-adenosyl-<span style="font-variant: small-caps;">l</span>-methionine enzyme HydG lyses free tyrosine to produce <em>p</em>-cresol and the CO and CN<sup>−</sup> ligands of the [2Fe]<sub>H</sub> cluster. Here, we applied stopped-flow Fourier transform infrared and electron-nuclear double resonance spectroscopies to probe the formation of HydG-bound Fe-containing species bearing CO and CN<sup>−</sup> ligands with spectroscopic signatures that evolve on the 1- to 1000-second time scale. Through study of the <sup>13</sup>C, <sup>15</sup>N, and <sup>57</sup>Fe isotopologs of these intermediates and products, we identify the final HydG-bound species as an organometallic Fe(CO)<sub>2</sub>(CN) synthon that is ultimately transferred to apohydrogenase to form the [2Fe]<sub>H</sub> component of the H-cluster. |
| first_indexed | 2024-03-07T04:59:26Z |
| format | Journal article |
| id | oxford-uuid:d7c3b52e-45b1-40a3-a13c-4d41d5157424 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:59:26Z |
| publishDate | 2014 |
| publisher | American Association for the Advancement of Science |
| record_format | dspace |
| spelling | oxford-uuid:d7c3b52e-45b1-40a3-a13c-4d41d51574242022-03-27T08:43:25ZThe HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d7c3b52e-45b1-40a3-a13c-4d41d5157424EnglishSymplectic Elements at OxfordAmerican Association for the Advancement of Science2014Kuchenreuther, JMyers, WSuess, DStich, TPelmenschikov, VShiigi, SACramer, SSwartz, JRBritt, RGeorge, SThree iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]<sub>H</sub> component of the catalytic H-cluster of FeFe hydrogenase. The radical <em>S</em>-adenosyl-<span style="font-variant: small-caps;">l</span>-methionine enzyme HydG lyses free tyrosine to produce <em>p</em>-cresol and the CO and CN<sup>−</sup> ligands of the [2Fe]<sub>H</sub> cluster. Here, we applied stopped-flow Fourier transform infrared and electron-nuclear double resonance spectroscopies to probe the formation of HydG-bound Fe-containing species bearing CO and CN<sup>−</sup> ligands with spectroscopic signatures that evolve on the 1- to 1000-second time scale. Through study of the <sup>13</sup>C, <sup>15</sup>N, and <sup>57</sup>Fe isotopologs of these intermediates and products, we identify the final HydG-bound species as an organometallic Fe(CO)<sub>2</sub>(CN) synthon that is ultimately transferred to apohydrogenase to form the [2Fe]<sub>H</sub> component of the H-cluster. |
| spellingShingle | Kuchenreuther, J Myers, W Suess, D Stich, T Pelmenschikov, V Shiigi, SA Cramer, S Swartz, JR Britt, R George, S The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title | The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title_full | The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title_fullStr | The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title_full_unstemmed | The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title_short | The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster. |
| title_sort | hydg enzyme generates an fe co 2 cn synthon in assembly of the fefe hydrogenase h cluster |
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