Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase
Ferredoxin-thioredoxinreductase is an essential member of a light-dependent regulatory system in oxygenic photosynthesis. This enzyme is composed of two nonidentical subunits, contains a 4Fe-4S cluster of a yet unknown function, and a catalytically active dithiol group. We have used N-ethy...
| Main Authors: | , |
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| Format: | Article |
| Language: | deu |
| Published: |
Swiss Chemical Society
1993-06-01
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| Series: | CHIMIA |
| Online Access: | https://chimia.ch/chimia/article/view/2262 |
| _version_ | 1818296316636168192 |
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| author | Peter Schiirmann Laura Gardet-Salvi |
| author_facet | Peter Schiirmann Laura Gardet-Salvi |
| author_sort | Peter Schiirmann |
| collection | DOAJ |
| description |
Ferredoxin-thioredoxinreductase is an essential member of a light-dependent regulatory system in oxygenic photosynthesis. This enzyme is composed of two nonidentical subunits, contains a 4Fe-4S cluster of a yet unknown function, and a catalytically active dithiol group. We have used
N-ethylmaleimide to modify specifically the active site thiols of the protein and show that their chemical modification completely abolishes the catalytic capacity of the enzyme and causes changes in the absorption spectrum of the protein.
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| first_indexed | 2024-12-13T04:01:36Z |
| format | Article |
| id | doaj.art-5a256d56806048ab8d5a8837649583a9 |
| institution | Directory Open Access Journal |
| issn | 0009-4293 2673-2424 |
| language | deu |
| last_indexed | 2024-12-13T04:01:36Z |
| publishDate | 1993-06-01 |
| publisher | Swiss Chemical Society |
| record_format | Article |
| series | CHIMIA |
| spelling | doaj.art-5a256d56806048ab8d5a8837649583a92022-12-22T00:00:25ZdeuSwiss Chemical SocietyCHIMIA0009-42932673-24241993-06-01476Chemical Modification of the Active Site of Ferredoxin-Thioredoxin ReductasePeter SchiirmannLaura Gardet-Salvi Ferredoxin-thioredoxinreductase is an essential member of a light-dependent regulatory system in oxygenic photosynthesis. This enzyme is composed of two nonidentical subunits, contains a 4Fe-4S cluster of a yet unknown function, and a catalytically active dithiol group. We have used N-ethylmaleimide to modify specifically the active site thiols of the protein and show that their chemical modification completely abolishes the catalytic capacity of the enzyme and causes changes in the absorption spectrum of the protein. https://chimia.ch/chimia/article/view/2262 |
| spellingShingle | Peter Schiirmann Laura Gardet-Salvi Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase CHIMIA |
| title | Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase |
| title_full | Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase |
| title_fullStr | Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase |
| title_full_unstemmed | Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase |
| title_short | Chemical Modification of the Active Site of Ferredoxin-Thioredoxin Reductase |
| title_sort | chemical modification of the active site of ferredoxin thioredoxin reductase |
| url | https://chimia.ch/chimia/article/view/2262 |
| work_keys_str_mv | AT peterschiirmann chemicalmodificationoftheactivesiteofferredoxinthioredoxinreductase AT lauragardetsalvi chemicalmodificationoftheactivesiteofferredoxinthioredoxinreductase |