Regulation of the Primary Quinone Binding Conformation
by the H Subunit in Reaction Centers from Rhodobacter
sphaeroides
Version 3 2015-11-20, 12:07
Version 2 2015-11-20, 12:07
Version 1 2015-11-20, 12:07
Posted on 2015-11-20 - 12:07
Unlike photosystem II (PSII) in higher
plants, bacterial photosynthetic
reaction centers (bRCs) from Proteobacteria have an additional peripheral membrane subunit “H”.
The H subunit is necessary for photosynthetic growth, but can be removed
chemically in vitro. The remaining LM dimer retains
its activity to perform light-induced charge separation. Here we investigate
the influence of the H subunit on interactions between the primary
semiquinone and the protein matrix, using a combination of site-specific
isotope labeling, pulsed electron paramagnetic resonance (EPR), and
density functional theory (DFT) calculations. The data reveal substantially
weaker binding interactions between the primary semiquinone and the
LM dimer than observed for the intact bRC; the amount of electron
spin transferred to the nitrogen hydrogen bond donors is significantly
reduced, the methoxy groups are more free to rotate, and the spectra
indicate a heterogeneous mixture of bound semiquinone states. These
results are consistent with a loosening of the primary quinone binding
pocket in the absence of the H subunit.
CITE THIS COLLECTION
DataCite
3 Biotech
3D Printing in Medicine
3D Research
3D-Printed Materials and Systems
4OR
AAPG Bulletin
AAPS Open
AAPS PharmSciTech
Abhandlungen aus dem Mathematischen Seminar der Universität Hamburg
ABI Technik (German)
Academic Medicine
Academic Pediatrics
Academic Psychiatry
Academic Questions
Academy of Management Discoveries
Academy of Management Journal
Academy of Management Learning and Education
Academy of Management Perspectives
Academy of Management Proceedings
Academy of Management Review
Sun, Chang; Taguchi, Alexander
T.; Beal, Nathan
J.; O’Malley, Patrick J.; Dikanov, Sergei A.; Wraight, Colin A. (2015). Regulation of the Primary Quinone Binding Conformation
by the H Subunit in Reaction Centers from Rhodobacter
sphaeroides. ACS Publications. Collection. https://doi.org/10.1021/acs.jpclett.5b01851
or
Select your citation style and then place your mouse over the citation text to select it.
SHARE
Usage metrics
Read the peer-reviewed publication
AUTHORS (6)
CS
Chang Sun
AT
Alexander
T. Taguchi
NB
Nathan
J. Beal
PO
Patrick J. O’Malley
SD
Sergei A. Dikanov
CW
Colin A. Wraight