Mitochondrial organization

The decline in immune function may pardy depend on a deficiency of coenzyme Q, a group of closely related quinone compounds (ubiquinones) that participate in the mitochondrial electron transport chain (49). Concentrations of coenzyme Q (specifically coenzyme Q q) appear to decline with age in several organs, most notably the thymus. 

The thylakoid membrane is asymmetrically organized, or sided, like the mitochondrial membrane. It also shares the property of being a barrier to the passive diffusion of H ions. Photosynthetic electron transport thus establishes an electrochemical gradient, or proton-motive force, across the thylakoid membrane with the interior, or lumen, side accumulating H ions relative to the stroma of the chloroplast. Like oxidative phosphorylation, the mechanism of photophosphorylation is chemiosmotic. 

Figure 1 shows the phylogenetic relationship of the mitochondrial and bacterial Rieske proteins. Plant mitochondrial Rieske proteins form a separate cluster, whereas bacterial Rieske proteins are more closely related to Rieske proteins from fungi or mammals, although the subunit composition and organization of the bci complex is compa-... 

ATP certainly fulfils the criteria for a NT. It is mostly synthesised by mitochondrial oxidative phosphorylation using glucose taken up by the nerve terminal. Much of that ATP is, of course, required to help maintain Na+/K+ ATPase activity and the resting membrane potential as well as a Ca +ATPase, protein kinases and the vesicular binding and release of various NTs. But that leaves some for release as a NT. This has been shown in many peripheral tissues and organs with sympathetic and parasympathetic innervation as well as in brain slices, synaptosomes and from in vivo studies with microdialysis and the cortical cup. There is also evidence that in sympathetically innervated tissue some extracellular ATP originates from the activated postsynaptic cell. While most of the released ATP comes from vesicles containing other NTs, some... 

Anderson S, Bankier AT, Barrell BG, deBrujin MHL, Coulson AR, Drouin J, Eperon IC, Nieruch dp. Roe BA, Sanger F, Schreier PH, Smith AJH, Staden R and Young IG (1981) Sequence and organization of the human mitochondrial genome. Nature 290 457-465. 

GMBS or sulfo-GMBS have been used for studying carnitine palmitoyltransferase-1 in its formation of a complex within the outer mitochondrial membrane (Faye et al., 2007), for investigating protein organization of the postsynaptic density (Liu et al., 2006), and in studying the structure and dynamics of rhodopsin (Jacobsen et al., 2006). 

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