Early Steps in Bacterial Photosynthesis. Comparison of Three Mechanisms

1988 ◽  
pp. 389-398 ◽  
Author(s):  
R. A. Marcus
Keyword(s):  
Bacterial Photosynthesis

On the mechanism of cytochrome oxidation in bacterial photosynthesis

FEBS Letters ◽  
1986 ◽  
Vol 200 (2) ◽  
pp. 303-308 ◽  
Author(s):  
Mordechai Bixon ◽  
Joshua Jortner
Keyword(s):  
Bacterial Photosynthesis ◽  
Cytochrome Oxidation

Structural requirements of quinone coenzymes for endogenous and dye-mediated coupled electron transport in bacterial photosynthesis

1980 ◽  
Vol 12 (3-4) ◽  
pp. 95-110 ◽  
Author(s):  
A. Baccarini-Melandri ◽  
N. Gabellini ◽  
B. A. Melandri ◽  
E. Hurt ◽  
G. Hauska
Keyword(s):  
Electron Transport ◽  
Bacterial Photosynthesis ◽  
Structural Requirements

scholarly journals Dissecting the cytochrome c2–reaction centre interaction in bacterial photosynthesis using single molecule force spectroscopy

2019 ◽  
Vol 476 (15) ◽  
pp. 2173-2190
Author(s):  
Cvetelin Vasilev ◽  
Guy E. Mayneord ◽  
Amanda A. Brindley ◽  
Matthew P. Johnson ◽  
C. Neil Hunter
Keyword(s):  
Single Molecule ◽  
Silicon Oxide ◽  
Fluorescent Protein ◽  
Dissociation Constants ◽  
Force Spectroscopy ◽  
Spectroscopic Studies ◽  
Bacterial Photosynthesis ◽  
Dynamic Force ◽  
Reaction Centre ◽  
Cytochrome C2

Abstract The reversible docking of small, diffusible redox proteins onto a membrane protein complex is a common feature of bacterial, mitochondrial and photosynthetic electron transfer (ET) chains. Spectroscopic studies of ensembles of such redox partners have been used to determine ET rates and dissociation constants. Here, we report a single-molecule analysis of the forces that stabilise transient ET complexes. We examined the interaction of two components of bacterial photosynthesis, cytochrome c2 and the reaction centre (RC) complex, using dynamic force spectroscopy and PeakForce quantitative nanomechanical imaging. RC–LH1–PufX complexes, attached to silicon nitride AFM probes and maintained in a photo-oxidised state, were lowered onto a silicon oxide substrate bearing dispersed, immobilised and reduced cytochrome c2 molecules. Microscale patterns of cytochrome c2 and the cyan fluorescent protein were used to validate the specificity of recognition between tip-attached RCs and surface-tethered cytochrome c2. Following the transient association of photo-oxidised RC and reduced cytochrome c2 molecules, retraction of the RC-functionalised probe met with resistance, and forces between 112 and 887 pN were required to disrupt the post-ET RC–c2 complex, depending on the retraction velocities used. If tip-attached RCs were reduced instead, the probability of interaction with reduced cytochrome c2 molecules decreased 5-fold. Thus, the redox states of the cytochrome c2 haem cofactor and RC ‘special pair’ bacteriochlorophyll dimer are important for establishing a productive ET complex. The millisecond persistence of the post-ET cytochrome c2[oxidised]–RC[reduced] ‘product’ state is compatible with rates of cyclic photosynthetic ET, at physiologically relevant light intensities.

Energetics of Bacterial Photosynthesis

2009 ◽  
Vol 113 (36) ◽  
pp. 12424-12437 ◽  
Author(s):  
David N. LeBard ◽  
Dmitry V. Matyushov
Keyword(s):  
Bacterial Photosynthesis
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