The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.
The two cyanide ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine. Using selectively labeled tyrosine substrates, the cyanides were isotopically labeled via a recently developed in vitro maturation procedure allowing advanced electron paramagnetic resonance t...
| Päätekijät: | , , , , , |
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| Aineistotyyppi: | Journal article |
| Kieli: | English |
| Julkaistu: |
American Chemical Society
2014
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| _version_ | 1826281000315912192 |
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| author | Myers, W Stich, T Suess, D Kuchenreuther, J Swartz, JR Britt, R |
| author_facet | Myers, W Stich, T Suess, D Kuchenreuther, J Swartz, JR Britt, R |
| author_sort | Myers, W |
| collection | OXFORD |
| description | The two cyanide ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine. Using selectively labeled tyrosine substrates, the cyanides were isotopically labeled via a recently developed in vitro maturation procedure allowing advanced electron paramagnetic resonance techniques to probe the electronic structure of the catalytic core of the enzyme. The ratio of the isotropic (13)C hyperfine interactions for the two CN(-) ligands-a reporter of spin density on their respective coordinating iron ions-collapses from ≈5.8 for the Hox form of hydrogenase to <2 for the CO-inhibited form. Additionally, when the maturation was carried out using [(15)N]-tyrosine, no features previously ascribed to the nitrogen of the bridging dithiolate ligand were observed suggesting that this bridge is not sourced from tyrosine. |
| first_indexed | 2024-03-07T00:22:11Z |
| format | Journal article |
| id | oxford-uuid:7cef95cf-e65e-4044-9802-6d0f907d760d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:22:11Z |
| publishDate | 2014 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | oxford-uuid:7cef95cf-e65e-4044-9802-6d0f907d760d2022-03-26T21:00:08ZThe cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7cef95cf-e65e-4044-9802-6d0f907d760dEnglishSymplectic Elements at OxfordAmerican Chemical Society2014Myers, WStich, TSuess, DKuchenreuther, JSwartz, JRBritt, RThe two cyanide ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine. Using selectively labeled tyrosine substrates, the cyanides were isotopically labeled via a recently developed in vitro maturation procedure allowing advanced electron paramagnetic resonance techniques to probe the electronic structure of the catalytic core of the enzyme. The ratio of the isotropic (13)C hyperfine interactions for the two CN(-) ligands-a reporter of spin density on their respective coordinating iron ions-collapses from ≈5.8 for the Hox form of hydrogenase to <2 for the CO-inhibited form. Additionally, when the maturation was carried out using [(15)N]-tyrosine, no features previously ascribed to the nitrogen of the bridging dithiolate ligand were observed suggesting that this bridge is not sourced from tyrosine. |
| spellingShingle | Myers, W Stich, T Suess, D Kuchenreuther, J Swartz, JR Britt, R The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title | The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title_full | The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title_fullStr | The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title_full_unstemmed | The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title_short | The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster. |
| title_sort | cyanide ligands of fefe hydrogenase pulse epr studies of 13 c and 15 n labeled h cluster |
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