The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping
Under anaerobic conditions Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a...
| Huvudupphovsmän: | , , , , , , |
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| Materialtyp: | Journal article |
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Portland Press
2018
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| _version_ | 1826299968662536192 |
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| author | Beaton, S Evans, R Finney, A Lamont, C Armstrong, F Sargent, F Carr, S |
| author_facet | Beaton, S Evans, R Finney, A Lamont, C Armstrong, F Sargent, F Carr, S |
| author_sort | Beaton, S |
| collection | OXFORD |
| description | Under anaerobic conditions Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from H2 oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly-bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein, HybB. To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In this paper we describe a new over-expression system that has facilitated determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex. |
| first_indexed | 2024-03-07T05:10:00Z |
| format | Journal article |
| id | oxford-uuid:db3cf24d-8162-40fc-a79b-52988c27fda6 |
| institution | University of Oxford |
| last_indexed | 2024-03-07T05:10:00Z |
| publishDate | 2018 |
| publisher | Portland Press |
| record_format | dspace |
| spelling | oxford-uuid:db3cf24d-8162-40fc-a79b-52988c27fda62022-03-27T09:09:05ZThe structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumpingJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:db3cf24d-8162-40fc-a79b-52988c27fda6Symplectic Elements at OxfordPortland Press2018Beaton, SEvans, RFinney, ALamont, CArmstrong, FSargent, FCarr, SUnder anaerobic conditions Escherichia coli is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from H2 oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly-bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein, HybB. To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In this paper we describe a new over-expression system that has facilitated determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex. |
| spellingShingle | Beaton, S Evans, R Finney, A Lamont, C Armstrong, F Sargent, F Carr, S The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title | The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title_full | The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title_fullStr | The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title_full_unstemmed | The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title_short | The structure of hydrogenase-2 from Escherichia coli: implications for H2 -driven proton pumping |
| title_sort | structure of hydrogenase 2 from escherichia coli implications for h2 driven proton pumping |
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