X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster
The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscop...
| Hlavní autoři: | , , , , , , |
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| Médium: | Journal article |
| Jazyk: | English |
| Vydáno: |
Royal Society of Chemistry
2018
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| _version_ | 1826302040095064064 |
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| author | Volbeda, A Mouesca, J Darnault, C Roessler, M Parkin, A Armstrong, F Fontecilla-Camps, J |
| author_facet | Volbeda, A Mouesca, J Darnault, C Roessler, M Parkin, A Armstrong, F Fontecilla-Camps, J |
| author_sort | Volbeda, A |
| collection | OXFORD |
| description | The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype. |
| first_indexed | 2024-03-07T05:41:28Z |
| format | Journal article |
| id | oxford-uuid:e5b6985c-a65d-4cfb-8345-e430c3897fc8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:41:28Z |
| publishDate | 2018 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | oxford-uuid:e5b6985c-a65d-4cfb-8345-e430c3897fc82022-03-27T10:26:01ZX-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] clusterJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e5b6985c-a65d-4cfb-8345-e430c3897fc8EnglishSymplectic Elements at OxfordRoyal Society of Chemistry2018Volbeda, AMouesca, JDarnault, CRoessler, MParkin, AArmstrong, FFontecilla-Camps, JThe crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype. |
| spellingShingle | Volbeda, A Mouesca, J Darnault, C Roessler, M Parkin, A Armstrong, F Fontecilla-Camps, J X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title | X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title_full | X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title_fullStr | X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title_full_unstemmed | X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title_short | X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster |
| title_sort | x ray structural functional and computational studies of the o2 sensitive e coli hydrogenase 1 c19g variant reveal an unusual 4fe 4s cluster |
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