Energy-transducing

The force-producing MAPs (kinesin, dynein, and dynamin) function as energy-transducing ATPases to provide the motive force for cilia and flagella by means of... 

Escher, B. I. Snozzi, M. Schwarzenbach, R. P, Uptake, speciation, and uncoupling activity of substituted phenols in energy transducing membranes, Environ. Sci. Technol. 30, 3071-3079 (1996). 

Biosensors will thus include a recognition element of biological nature, that allows the selective recognition of the analyte in the course of a biochemical reaction (chemical transduction), and an energy transducer (stemming from the latin word transducere, to lead across) that transforms... 

Uncoupling is a specific toxic effect that takes place in energy-transducing membranes (photosynthetically active membranes, inner mitochondrial... 

Fig. 2. Fluid mosaic model of an energy transducing membrane...

Foster DL, Fillingame RH. 1979. Energy-transducing H -ATPase of Escherichia colt purification, reconstitution and subunit composition. J Biol Chem 254 8230-6. 

Mitochondrial responses. Studies similar to those Involving isolated chloroplasts and thylakoids were conducted with isolated mung bean mitochondria in order to ascertain whether the effects imposed on thylakoid membranes were common to energy transducing membranes in general. 

J-L Rigaud, B Pitard, D Levy. Reconstitution of membrane proteins into liposomes application to energy-transducing membrane proteins. Biochim Biophys Acta 1231 223-246, 1995. 

As an attempt to connect the first discussion, which was concerned with diffusion-reaction coupling, with Dr. Williams presentation of enzymes as dynamic systems, I wanted to direct attention to a number of specific systems. These are the energy-transducing proteins that couple scalar chemical reactions to vectorial flow processes. For example, I am thinking of active transport (Na-K ATPase), muscular contraction (actomyosin ATPase), and the light-driven proton pump of the well-known purple... 

One striking characteristic of the coupling ATPase of energy-transducing membranes, apart from the extraordinarily large number of different polypeptide subunits, is the existence of two different polypeptides involved in the response of the enzyme to the inhibitor oligomycin. One binds the inhibitor, the other, separated in space from the former by possibly as much as 10 to 15 A, confers oligomycin sensitivity to the entire enzyme complex. How could the transfer of information between these two polypeptide subunits and their concerted interaction with the ATPase proper be visualized ... 

We really do not have energy sources as such in nature, even though we sloppily use that term. Instead, we actually have energy transducers. Else we must discard the conservation of energy law itself Energy can neither be created nor destroyed, but only changed in form. 

Further, by the definition of broken symmetry, the proven asymmetry of the source dipole in the vacuum flux must receive virtual energy and output observable energy. Since we see only the 3-spatial output, to us it appears that the source dipole somehow extracts from the vacuum some unobservable energy, transduces it, and then pours it out as the observable EM energy that we do observe. 

Hence the charge receives the complex convergent EM energy, transduces it into real EM energy, and emits enormous energy at the speed of light in all directions. 

The carriers in turn donate electrons to acceptors with higher electron affinities, with the release of energy. Cells contain a variety of molecular energy transducers, which convert the energy of electron flow into useful work. 

Since mitochondria are the site of high oxidative metabolism, they are under continual oxidative stress. In fact, it has been estimated that approximately 2 percent of mitochondrial 02 consumption generates ROS. The mitochondrial electron transfer chain is one of the main sources of ROS in aerobic cells, due to electron leakage from energy-transducing sequences leading to the formation of superoxide radicals. 

Yano T (2002) The energy-transducing NADH quinone oxidoreductase, complex I. Mol Asp Med 23 345-368... 

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