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    Improved membrane permeability with cetyltrimethylammonium bromide (CTAB) addition for enhanced bidirectional transport of substrate and electron shuttles
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    Single-turnover electron transfer within the mitochondrial complex III has been studied by combining, in solution, the isolated complex from bovine heart with detergent-solubilized reaction centers of Rhodopseudomonas sphaeroides. Initiation of electron transfer by short flash activation resulted in the prompt oxidation of cytochrome c and reduction of cytochrome b. The subsequent reduction of ferricytochrome c was observed to be concomitant with the oxidation of the ferrocytochrome b, both reactions being inhibited by the addition of actimycin A. The rate of electron transfer through complex III is dependent upon the ambient redox potential poise in a way that is consistent with the presence of a redox component, presumably analogous to the photosynthetic ubiquinone Qz, which is an obligatory intermediate in electron transfer between cytochromes b and c. These results demonstrate cyclic electron transfer in a constructed assembly of mitochondrial complex III, cytochrome c, and photochemical reaction centers.
    Cytochrome C1
    Cytochrome b6f complex
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    Copper nanoparticles were synthesized in a nonaqueous solution of cetyltrimethylammonium bromide with isopropanol as a solvent. Cetyltrimethylammonium bromide in isopropanol is observed to play a role as a catalyst where isopropanol is the reducing agent. The surface plasmon band characteristic for Cu nanoparticles can be observed at approximately 560 nm in the UV-visible spectra at molar ratios for Cu2+: cetyltrimethylammonium bromide of 1:15 and 1:30. On the other hand, at molar ratios of 1:0.25 and 1:1 the presence of peak at approximately 310 nm can be attributed to oligomeric clusters of Cu0. Formation of Cu0 was further confirmed from the X-ray diffraction analysis. The diffractograms exhibited peaks at 2theta = approximately 41.6 degrees, approximately 51.6 degrees, and approximately 74.3 degrees, corresponding to Cu0. At lower concentration of cetyltrimethylammonium bromide (i.e., Cu2+: cetyltrimethylammonium bromide = 1:0.25) higher degree of size dispersity (particles between approximately 5-20 nm) can be noted from transmission electron micrograph. On the other hand, at the highest concentration of cetyltrimethylammonium bromide (i.e., Cu2+: cetyltrimethylammonium bromide = 1:30), formation of finer sized particles with a lower degree of size variation, approximately 2-10 nm, can be observed.
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    All biological energy (and, thus, all fossil energy) is ultimately derived from a series of basic electron transfer reactions, starting with the primary charge separation in photosynthesis. The subsequent energy flow proceeds through a series of subsequent redox reactions, largely involving metallo-proteins in which the energy of reduction is coupled to proton transport and manufacture of ATP for biosyntheses. (Fig 1). 1Mitochondral electron transport chain. Despite the obvious importance of such redox reactions, until recently such reactions remained rather poorly characterised, and poorly understood. Within the past few years, however, rapid advances have occurred in several key areas, including: 1) electron transfer theory1-3 2) experiments on model reactions (eg: electron transfer at long, fixed distance),4-6 3) experimental techniques for monitoring rapid biological electron transfer,7-10 and 4) structural charaterization of the redox proteins themselves,11-15 including detailed models for the protein-protein complexes within which electron transfer occurs. As a result of these advances, rapid experimental
    Electron flow
    Proton-Coupled Electron Transfer