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(1)H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site
[Image: see text] The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using (1)H NMR spectroscopy identifying the paramagnetically shifted (1)H resonances associated with both the [4Fe-4S](H) and the [2Fe](H) subclusters of the active site “H-cluster”. The signal pattern of...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5765528/ https://www.ncbi.nlm.nih.gov/pubmed/29211457 http://dx.doi.org/10.1021/jacs.7b11196 |
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author | Rumpel, Sigrun Ravera, Enrico Sommer, Constanze Reijerse, Edward Farès, Christophe Luchinat, Claudio Lubitz, Wolfgang |
author_facet | Rumpel, Sigrun Ravera, Enrico Sommer, Constanze Reijerse, Edward Farès, Christophe Luchinat, Claudio Lubitz, Wolfgang |
author_sort | Rumpel, Sigrun |
collection | PubMed |
description | [Image: see text] The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using (1)H NMR spectroscopy identifying the paramagnetically shifted (1)H resonances associated with both the [4Fe-4S](H) and the [2Fe](H) subclusters of the active site “H-cluster”. The signal pattern of the unmaturated HydA1 containing only [4Fe-4S](H) is reminiscent of bacterial-type ferredoxins. The spectra of maturated HydA1, with a complete H-cluster in the active H(ox) and the CO-inhibited H(ox)–CO state, reveal additional upfield and downfield shifted (1)H resonances originating from the four methylene protons of the azadithiolate ligand in the [2Fe](H) subsite. The two axial protons are affected by positive spin density, while the two equatorial protons experience negative spin density. These protons can be used as important probes sensing the effects of ligand-binding to the catalytic site of the H-cluster. |
format | Online Article Text |
id | pubmed-5765528 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-57655282018-01-14 (1)H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site Rumpel, Sigrun Ravera, Enrico Sommer, Constanze Reijerse, Edward Farès, Christophe Luchinat, Claudio Lubitz, Wolfgang J Am Chem Soc [Image: see text] The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using (1)H NMR spectroscopy identifying the paramagnetically shifted (1)H resonances associated with both the [4Fe-4S](H) and the [2Fe](H) subclusters of the active site “H-cluster”. The signal pattern of the unmaturated HydA1 containing only [4Fe-4S](H) is reminiscent of bacterial-type ferredoxins. The spectra of maturated HydA1, with a complete H-cluster in the active H(ox) and the CO-inhibited H(ox)–CO state, reveal additional upfield and downfield shifted (1)H resonances originating from the four methylene protons of the azadithiolate ligand in the [2Fe](H) subsite. The two axial protons are affected by positive spin density, while the two equatorial protons experience negative spin density. These protons can be used as important probes sensing the effects of ligand-binding to the catalytic site of the H-cluster. American Chemical Society 2017-12-06 2018-01-10 /pmc/articles/PMC5765528/ /pubmed/29211457 http://dx.doi.org/10.1021/jacs.7b11196 Text en Copyright © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Rumpel, Sigrun Ravera, Enrico Sommer, Constanze Reijerse, Edward Farès, Christophe Luchinat, Claudio Lubitz, Wolfgang (1)H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site |
title | (1)H NMR Spectroscopy of [FeFe] Hydrogenase:
Insight into the Electronic Structure of the Active Site |
title_full | (1)H NMR Spectroscopy of [FeFe] Hydrogenase:
Insight into the Electronic Structure of the Active Site |
title_fullStr | (1)H NMR Spectroscopy of [FeFe] Hydrogenase:
Insight into the Electronic Structure of the Active Site |
title_full_unstemmed | (1)H NMR Spectroscopy of [FeFe] Hydrogenase:
Insight into the Electronic Structure of the Active Site |
title_short | (1)H NMR Spectroscopy of [FeFe] Hydrogenase:
Insight into the Electronic Structure of the Active Site |
title_sort | (1)h nmr spectroscopy of [fefe] hydrogenase:
insight into the electronic structure of the active site |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5765528/ https://www.ncbi.nlm.nih.gov/pubmed/29211457 http://dx.doi.org/10.1021/jacs.7b11196 |
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