Membranes energy transfer

ILIEVA A, IVANOV A G, KOVACHEV K and RICHTER H p (1992) Cryodamage in ram sperm plasma membranes. Energy transfer and freeze-fracture studies. Bioelectrochem Bioenerg, 27,41-44. 

Modeling of the reaction center inside the hole of LHl shows that the primary photon acceptor—the special pair of chlorophyll molecules—is located at the same level in the membrane, about 10 A from the periplasmic side, as the 850-nm chlorophyll molecules in LH2, and by analogy the 875-nm chlorophyll molecules of LHl. Furthermore, the orientation of these chlorophyll molecules is such that very rapid energy transfer can take place within a plane parallel to the membrane surface. The position and orientation of the chlorophyll molecules in these rings are thus optimal for efficient energy transfer to the reaction center. 

From here the water mixture rises through the water-wall tubes (generator tubes) that constitute the furnace membrane where steam is generated (primarily by radiant energy transfer). The steam-BW mixture is collected in top water-wall headers and conducted through risers (riser tubes) back to the top drum, where the saturated steam separates from the water at the steam-water interface. 

A number of transport mediators are transport proteins in the absence of an external energy supply, thermal motion leads to their conformational change or rotation so that the transported substance, bound at one side of the membrane, is transferred to the other side of the membrane. This type of mediator has a limited number of sites for binding the transported substance, so that an increase in the concentration of the latter leads to saturation. Here, the transport process is characterized by specificity for a given substance and inhibition by other transportable substances competing for binding sites and also by various inhibitors. When the concentrations of the transported substance are identical on both sides of the membrane,... 

In pure water, electron or energy transfer to carotenoid aggregates is obstructed by the membrane of outside-directed polar groups (Sliwka et al. 2007), Figure 3.14. 

Mattjus, P., Molotkovsky, J. G., Smaby, J. M. and Brown, R. E. (1999). A fluorescence resonance energy transfer approach for monitoring protein-mediated glycolipid transfer between vesicle membranes. Anal. Biochem. 268, 297-304. 

Verbist, J., Gadella, T. W. J., Raeymaekers, L., Wuytack, F., Wirtz, K. W. A. and Casteels, R. (1991). Phosphoinositide-protein Interactions of the plasma-membrane Ca2+-transport ATPase as revealed by fluorescence energy-transfer. Biochim. Biophys. Acta 1063, 1-6. 

Fung, B. K. and Stryer, L. (1978). Surface density determination in membranes by fluorescence energy transfer. Biochemistry 17, 5241-8. 

The upgrade of a frequency-domain fluorescence lifetime imaging microscope (FLIM) to a prismless objective-based total internal reflection-FLIM (TIR-FLIM) system is described. By off-axis coupling of the intensity-modulated laser from a fiber and using a high numerical aperture oil objective, TIR-FLIM can be readily achieved. The usefulness of the technique is demonstrated by a fluorescence resonance energy transfer study of Annexin A4 relocation and two-dimensional crystal formation near the plasma membrane of cultured mammalian cells. Possible future applications and comparison to other techniques are discussed. 

Khakh, B. S., Fisher, J. A., Nashmi, R., Bowser, D. N. and Lester, H. A. (2005). An angstrom scale interaction between plasma membrane ATP-gated P2X2 and alpha4beta2 nicotinic channels measured with fluorescence resonance energy transfer and total internal reflection fluorescence microscopy. J. Neurosci. 25, 6911-20. 

Silvius, J. R. and Nabi, I. R. (2006). Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes. Mol. Membr. Biol. 23, 5-16. 

Maurel, D., Kniazeff, J., Mathis, G., Trinquet, E., Pin, J. P. and Ansanay, FI. (2004). Cell surface detection of membrane protein interaction with homogeneous time-resolved fluorescence resonance energy transfer technology. Anal. Biochem. 329, 253-62. 

Fehr, M., Takanaga, H., Ehrhardt, D. W. and Frommer, W. B. (2005b). Evidence for high-capacity bidirectional glucose transport across the endoplasmic reticulum membrane by genetically encoded fluorescence resonance energy transfer nanosensors. Mol. Cell. Biol. 25, 11102-12. 

Posokhov, Y. O., Merzlyakov, M., Hristova, K. and Ladokhin, A. S. (2008). A simple proximity correction for Forster resonance energy transfer efficiency determination in membranes using lifetime measurements. Anal. Biochem. 380, 134—6. 

Isaacs, B.S., Husten, E.J., Esmon, C.T., and Johnson, A.E. (1986) A domain of membrane-bound blood coagulation factor Va is located far from the phospholipid surface. A fluorescence energy transfer measurement. Biochemistry 25, 4958-4969. 

The photosynthetic reaction center (RC) of purple nonsulfur bacteria is the core molecular assembly, located in a membrane of the bacteria, that initiates a series of electron transfer reactions subsequent to energy transfer events. The bacterial photosynthetic RCs have been characterized in more detail, both structurally and functionally, than have other transmembrane protein complexes [1-52]. 

The lack of selectivity can be circumvented by coupling a postcolumn flow system to a liquid chromatograph. This has promoted the development of a number of efficient liquid chromatography-CL approaches [16, 17]. Eluted analytes are mixed with streams of the substrate and oxidant (in the presence or absence of a catalyst or inhibitor) and the mixed stream is driven to a planar coiled flow cell [18] or sandwich membrane cell [19] in an assembly similar to those of flow injection-CL systems. Many of these postcolumn flow systems are based on an energy-transfer CL process [20], In others, the analytes are mixtures of metal ions and the luminol-hydrogen peroxide system is used to generate the luminescence [21],... 

Adkins, C. E., Pillai, G. V., Kerby, J., et al. (2001) alpha4beta3delta GABA(A) receptors characterized by fluorescence resonance energy transfer-derived measurements of membrane potential. J. Biol. Chem. 276, 38934-38939. 

Figure 1. Schematic representation of the artificial photosynthetic reaction center by a monolayer assembly by A-S-D triad and antenna molecules for light harvesting (H), lateral energy migration and energy transfer, and charge separation across the membrane via multistep electron transfer (a) Side view of mono-layer assembly, (b) top view of a triad surrounded by H molecules, and (c) energy diagram for photo-electric conversion in a monolayer assembly.

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