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Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM
Movement of the Rieske domain of the iron–sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII(2) from Yarr...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9812224/ https://www.ncbi.nlm.nih.gov/pubmed/36598500 http://dx.doi.org/10.1107/S2052252522010570 |
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author | Wieferig, Jan-Philip Kühlbrandt, Werner |
author_facet | Wieferig, Jan-Philip Kühlbrandt, Werner |
author_sort | Wieferig, Jan-Philip |
collection | PubMed |
description | Movement of the Rieske domain of the iron–sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII(2) from Yarrowia lipolytica at resolutions up to 2.0 Å under different conditions, with different redox states of the cofactors of the high-potential chain. All possible permutations of three primary positions were observed, indicating that the two halves of the dimeric complex act independently. Addition of the substrate analogue decylubiquinone to CIII(2) with a reduced high-potential chain increased the occupancy of the Q(o) site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c (1) subunits varied depending on the redox state and substrate. In the absence of quinols, the reduced Rieske domain interacted more closely with cytochrome b and cytochrome c (1) than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd (1)-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain. |
format | Online Article Text |
id | pubmed-9812224 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-98122242023-01-09 Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM Wieferig, Jan-Philip Kühlbrandt, Werner IUCrJ Research Papers Movement of the Rieske domain of the iron–sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII(2) from Yarrowia lipolytica at resolutions up to 2.0 Å under different conditions, with different redox states of the cofactors of the high-potential chain. All possible permutations of three primary positions were observed, indicating that the two halves of the dimeric complex act independently. Addition of the substrate analogue decylubiquinone to CIII(2) with a reduced high-potential chain increased the occupancy of the Q(o) site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c (1) subunits varied depending on the redox state and substrate. In the absence of quinols, the reduced Rieske domain interacted more closely with cytochrome b and cytochrome c (1) than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd (1)-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain. International Union of Crystallography 2023-01-01 /pmc/articles/PMC9812224/ /pubmed/36598500 http://dx.doi.org/10.1107/S2052252522010570 Text en © Jan-Philip Wieferig et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Papers Wieferig, Jan-Philip Kühlbrandt, Werner Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title | Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title_full | Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title_fullStr | Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title_full_unstemmed | Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title_short | Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III(2) by cryo-EM |
title_sort | analysis of the conformational heterogeneity of the rieske iron–sulfur protein in complex iii(2) by cryo-em |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9812224/ https://www.ncbi.nlm.nih.gov/pubmed/36598500 http://dx.doi.org/10.1107/S2052252522010570 |
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