Mechanisms of energy coupling in Rhodopseudomonas capsulata by John Frederick Myatt Download PDF EPUB FB2
Rhodobacter capsulatus is a species of purple bacteria, a group of bacteria that can obtain energy through name is derived from the Latin adjective "capsulatus" ("with a chest", "encapsulated"), itself derived Latin noun "capsula" (meaning "a small box or chest"), and the associated Latin suffix for masculine nouns, "-atus" (denoting that something is "provided with Class: Alphaproteobacteria.
iosmotic coupling hypothesis, in whieh it is pro- posed that, at least in the steady state, the energy- coupling protons come into equilibrium with the electrochemical potential difference of H + be- tween the bulk aqueous phases that the coupling membrane serves to separate (e.g., see Refs.
Journals & Books; Help Download full Photophosphorylation in chromatophores from Rhodopseudomonas capsulata is potently uncoupled by the protonophore SF Yet the uncoupling potency of this compound is actually further increased when the rate of phosphorylation in the absence of protonophore is decreased by the addition of the energy Cited by: Abstract.
Photosynthetic growth of Rhodopseudomonas capsulata, a nonsulfur purple bacterium, is severely inhibited by inorganic arsenate when this anion is present equimolar to orthophosphate in the culture s on an arsenate-resistant mutant indicate that its resistance can be explained by a significantly increased photophosphorylation capacity of the energy-converting machinery Cited by: Rhodopseudomonas capsulata).
The aim pursued by these studies, beyond the mere extension of previous researches on coupling factor proteins to prokaryotic photosynthetic organisms, was a comparison of the mechanism of photosynthetic and oxidative phos.
We discuss unique mechanisms typical in the elementary processes ofbiological functions. We focus on three topics. Excitation energytransfer in the light-harvesting antenna systems of photosyntheticbacteria is unique in its structure and the energy transfer mechanism.
Inthe case of LH2 of Rhodopseudomonas acidophila, the B intra-ringenergy transfer and the inter-ring energy. Inthe case of LH2 of Rhodopseudomonas acidophila, the B intra-ringenergy transfer and the inter-ring energy transfer between B and Btake place by the intermediate coupling mechanism of energy transfer.
Theexcitonic coherent domain shows a wave-like movement along the ring, andthis property is expected to play a significant role in the. Intact cells of Rhodopseudomonas capsulata, as photocatalyst for hydrogen production using light of λ> nm, were added to a slurry of naked or sensitized TiO 2 semiconductor containing MV 2+ as an electron relay.
It is discussed that the nitrogenase enzyme of the bacterial cells is responsible for catalyzing hydrogen production. Sensitization of TiO 2 was performed in three ways:.
Bakker EP, Harold FM. Energy coupling to potassium transport in Streptococcus faecalis. Interplay of ATP and the protonmotive force. J Biol Chem. Jan 25; (2)– [Google Scholar] Berger EA, Heppel LA.
Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli. Bakker EP, Harold FM.
Energy coupling to potassium transport in Streptococcus faecalis. Interplay of ATP and the protonmotive force. J Biol Chem. Jan 25; (2)– Berger EA, Heppel LA. Different mechanisms of energy coupling for the shock-sensitive and shock-resistant amino acid permeases of Escherichia coli.
The growth and maintenance of Rhodopseudomonas capsulata N22, It is concluded that the unit of energy coupling in bacterial chromatophores is much smaller than the entire coupling membrane.
Hitchens GD, Kell DB. Uncouplers can shuttle between localized energy-coupling sites during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N Biochem J.
Apr 15; (1)– [PMC free article] MITCHELL P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature. Figure shows the three-dimensional structure of the reaction center of the purple bacterium Rhodopseudomonas molecule has a cylindrical shape and is about 8 nm long.
The homologous subunits L (red) and M (black) are arranged symmetrically and enclose the chlorophyll and pheophytin molecules. The H subunit is attached like a lid to the lower part of the cylinder.
The Mechanism of the Ubiquinol: Cytochrome c Oxidoreductases of Mitochondria and of Rhodopseudomonas sphaeroides Crowther, D., Bowyer, J. R., and Tiemey, G. V.,Electron transport through the antimycin sensitive site in Rhodopseudomonas capsulata, in: Structure and Function of Energy-Transducing Systems (K.
van Dam and B. van. A lot of hypothetical schemes were put forward to explain the nature of coupling between electron transfer and phosphorylation, but none of them solved the problem.
Only quite recently, one hypo thetical scheme of energy coupling, viz. Mitchell's chemiosmotic concept, was supported by experimental data which allow us to prefer it to. An environmentally friendly method using a cell‐free extract (CFE) of Rhodopseudomonas capsulata is proposed to synthesize gold nanowires with a network structure.
This procedure offers control over the shapes of gold nanoparticles with the change of HAuCl 4 concentration. The CFE solutions were added with different concentrations of HAuCl 4, resulting in the bioreduction of gold ions and. Biophys. 94, (). Respiratory system 9) A. Baccarini Melandri, D.
Zannoni and B.A. Melandri, Energy transduction in photosynthetic bacteria. VI Respiratory sites of energy conservation in membranes from dark-grown cells of Rhodopseudomonas capsulata, Biochim. Biophys.
Acta(). The extent of the protonmotive force (transmembrane Δ H+ /F) developed in bacterial chromatophores from Rhodopseudomonas capsulata under continous illumination has been determined with measurements of the quenching of 9‐aminoacridine fluorescence and the red band shift of carotenoids.
The extent of the membrane potential generated in the dark with K + pulses in valinomycin‐treated. Hitchens GD, Kell DB. Localized energy coupling during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N Biosci Rep. Oct; 2 (10)– Hitchens GD, Kell DB.
Uncouplers can shuttle between localized energy-coupling sites during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N Uncouplers can shuttle between localized energy-coupling sites during photophosphorylation by chromatophores of Rhodopseudomonas capsulata N22 May Biochemical Journal (1) Hitchens, G.
and Kell, D. B, b, Localized energy coupling during photo phosphorylation by chromatophores of Rhodopseudomonas capsulata N22, Biosci., J, CrossRef Google Scholar Hitchens, G. and Kell, D.B, a, Uncouplers can shuttle between localized energy coupling sites during photo phosphorylation by chromatophores of.
This principle is applied to photophosphorylation by chromatophores from Rhodopseudomonas capsulata N 3. It is found that, in contrast to the predictions of the chemiosmotic coupling model, free energy transfer is confined to individual electron transport chain and ATP synthase complexes.
coupling factor does not play a significant role in the structural integrity of the particles. Resolution of a coupling factor by sonication in the presence of EDTA has been recently reported in chromatophores isolated from Rhodopseudomonas capsulata (10) and Rhodospirillum rubrum (11).
The contribution of each residue to the binding free energy was determined based on a per-residue decomposition scheme.
By calculating the five types of energies in each complex system, the most important three residues are listed in Table different complex with RPA, it is obvious that the most frequent occurrence residue is the Tyr, Trp and Met Abstract. Alternative energy-converting systems permit the nonsulfur purple photosynthetic bacterium Rhodopseudomonas capsulata to grow either with light or (dark) respiration as the source of energy.
Respiratory mutants, unable to grow aerobically in darkness, can be readily isolated and the defective step(s) in their respiratory mechanisms can be identified by study of biochemical activities. The Mechanism of R-Factor Mediated Arsenate Resistance Is an Inducible ATP-Driven Arsenate Efflux System Sodium Cycle: A Mechanism of Energy Coupling That Replaces the Proton Cycle in Marine Bacteria under Alkaline Conditions Role of Ion Gradients in Interaction of Basic Proteins and DNA with Model and Biological Membranes.
On the extent of localization of the energized membrane state in chromatophores from Rhodopseudomonas capsulata N22 Article (PDF Available) in Biochemical Journal (2) September Richard J.
Cogdell, J. Barry Jackson, Antony R. Crofts, The Effect of Redox Potential on the Coupling Between Rapid Hydrogen-Ion Binding and Electron Transport in Chromatophores from Rhodopseudomonas Spheroides, Membrane Structure and Mechanisms of Biological Energy Transduction, /, (), ().
Abstract. Previous work regarding solubilization, isolation and properties of coupling factors from mitochondria (PULLMAN et al.
I), chloroplasts (AVRONVAMBUTAS & RACKER ), and the oxidative system of certain bacteria (PINCHOTBRODIEISHIKAWA & LEHNINGER ) has led to some new insight into the fundamental mechanism of biological electron transport coupled energy.
Abstract. The activity of the light-dependent proton pump (in the absence of phosphorylation substrates) of Rhodopseudomonas capsulata „membrane vesicles,” in contrast to that of chloroplasts, is not appreciably affected by detachment of phosphorylation coupling factor(s).
Proton uptake by such „uncoupled” (low phosphorylation activity) preparations is also unaffected by the addition. Rhodospirillum rubrum and Rhodopseudomonas capsulata were able to grow anaerobically in the dark either by a strict mixed-acid fermentation of sugars or, in the presence of an appropriate electron acceptor, by an energy-linked anaerobic respiration.
Both species fermented fructose without the additi .Studies on the Mechanism of NAD-photoreduction by Chromatophores of the Facultative Phototroph, Rhodopseudomonas capsulata the relationships between cyclic photophosphorylation, light-induced noncyclic electron transport and energy-dependent NAD-reduction are discussed.The arsenic resistance mechanisms of a photosynthetic bacterium, Rhodopseudomonas palustris CQV97, under anaerobic and light conditions, were investigated in this study.