Inter-protein reactions of photosynthetic reaction centers (RCs) with bc1 complexes from R. sphaeroides, have been investigated using surface-enhanced Infrared-absorption spectroscopy (SEIRAS). Surface enhancement was achieved by a nano-structured gold surface. The proteins were immobilized via his-tags attached to the P side of the RC and the C-terminal end of the cytochrome (cyt) b subunit and co-reconstituted into a lipid bilayer by in-situ dialysis. In this configuration, the cyt c binding site of the two proteins is located on opposite sides of the membrane. Light-minus-dark absorbance spectra under continuous illumination in the absence of an electron donor indicated a slow quinone/semiquinone exchange, allowing release of ubiquinol (QH2) into the membrane. The interaction of the bc1 with QH2 was indicated by the stationary state obtained but only in the presence of cyt c. The interaction is discussed in terms of a semiquinone species formed in the course of the Q cycle mechanism of the bc1.
| Published in | International Journal of Bioorganic Chemistry (Volume 2, Issue 2) |
| DOI | 10.11648/j.ijbc.20170202.13 |
| Page(s) | 61-69 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2017. Published by Science Publishing Group |
Photosynthetic Reaction Centers, Bc1 Complexes, R. Sphaeroides, Surface-Enhanced Infrared-Absorption Spectroscopy, Nano-Structured Gold Surface, Ubiquinol, Semiquinone, His-Tags
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APA Style
Vedran Nedelkovski, Andreas Schwaighofer, Andreas F. Geiss, Christina Bliem, Renate L. C. Naumann. (2017). Interactions of Photosynthetic Reaction Centers with Bc1 Complexes from Rhodobacter Sphaeroides Studied Using SEIRAS on a Nano-Structured Gold Surface. International Journal of Bioorganic Chemistry, 2(2), 61-69. https://doi.org/10.11648/j.ijbc.20170202.13
ACS Style
Vedran Nedelkovski; Andreas Schwaighofer; Andreas F. Geiss; Christina Bliem; Renate L. C. Naumann. Interactions of Photosynthetic Reaction Centers with Bc1 Complexes from Rhodobacter Sphaeroides Studied Using SEIRAS on a Nano-Structured Gold Surface. Int. J. Bioorg. Chem. 2017, 2(2), 61-69. doi: 10.11648/j.ijbc.20170202.13
AMA Style
Vedran Nedelkovski, Andreas Schwaighofer, Andreas F. Geiss, Christina Bliem, Renate L. C. Naumann. Interactions of Photosynthetic Reaction Centers with Bc1 Complexes from Rhodobacter Sphaeroides Studied Using SEIRAS on a Nano-Structured Gold Surface. Int J Bioorg Chem. 2017;2(2):61-69. doi: 10.11648/j.ijbc.20170202.13
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Download@article{10.11648/j.ijbc.20170202.13,
author = {Vedran Nedelkovski and Andreas Schwaighofer and Andreas F. Geiss and Christina Bliem and Renate L. C. Naumann},
title = {Interactions of Photosynthetic Reaction Centers with Bc1 Complexes from Rhodobacter Sphaeroides Studied Using SEIRAS on a Nano-Structured Gold Surface},
journal = {International Journal of Bioorganic Chemistry},
volume = {2},
number = {2},
pages = {61-69},
doi = {10.11648/j.ijbc.20170202.13},
url = {https://doi.org/10.11648/j.ijbc.20170202.13},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijbc.20170202.13},
abstract = {Inter-protein reactions of photosynthetic reaction centers (RCs) with bc1 complexes from R. sphaeroides, have been investigated using surface-enhanced Infrared-absorption spectroscopy (SEIRAS). Surface enhancement was achieved by a nano-structured gold surface. The proteins were immobilized via his-tags attached to the P side of the RC and the C-terminal end of the cytochrome (cyt) b subunit and co-reconstituted into a lipid bilayer by in-situ dialysis. In this configuration, the cyt c binding site of the two proteins is located on opposite sides of the membrane. Light-minus-dark absorbance spectra under continuous illumination in the absence of an electron donor indicated a slow quinone/semiquinone exchange, allowing release of ubiquinol (QH2) into the membrane. The interaction of the bc1 with QH2 was indicated by the stationary state obtained but only in the presence of cyt c. The interaction is discussed in terms of a semiquinone species formed in the course of the Q cycle mechanism of the bc1.},
year = {2017}
}
TY - JOUR T1 - Interactions of Photosynthetic Reaction Centers with Bc1 Complexes from Rhodobacter Sphaeroides Studied Using SEIRAS on a Nano-Structured Gold Surface AU - Vedran Nedelkovski AU - Andreas Schwaighofer AU - Andreas F. Geiss AU - Christina Bliem AU - Renate L. C. Naumann Y1 - 2017/03/22 PY - 2017 N1 - https://doi.org/10.11648/j.ijbc.20170202.13 DO - 10.11648/j.ijbc.20170202.13 T2 - International Journal of Bioorganic Chemistry JF - International Journal of Bioorganic Chemistry JO - International Journal of Bioorganic Chemistry SP - 61 EP - 69 PB - Science Publishing Group SN - 2578-9392 UR - https://doi.org/10.11648/j.ijbc.20170202.13 AB - Inter-protein reactions of photosynthetic reaction centers (RCs) with bc1 complexes from R. sphaeroides, have been investigated using surface-enhanced Infrared-absorption spectroscopy (SEIRAS). Surface enhancement was achieved by a nano-structured gold surface. The proteins were immobilized via his-tags attached to the P side of the RC and the C-terminal end of the cytochrome (cyt) b subunit and co-reconstituted into a lipid bilayer by in-situ dialysis. In this configuration, the cyt c binding site of the two proteins is located on opposite sides of the membrane. Light-minus-dark absorbance spectra under continuous illumination in the absence of an electron donor indicated a slow quinone/semiquinone exchange, allowing release of ubiquinol (QH2) into the membrane. The interaction of the bc1 with QH2 was indicated by the stationary state obtained but only in the presence of cyt c. The interaction is discussed in terms of a semiquinone species formed in the course of the Q cycle mechanism of the bc1. VL - 2 IS - 2 ER -
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