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Transduction energy

Cramer W A and Knaff D B 1990 Energy Transduction in Biological Membranes (New York Springer)... [Pg.2994]

Metabolic Functions. The functions of the thyroid hormones and thus of iodine are control of energy transductions (121). These hormones increase oxygen consumption and basal metaboHc rate by accelerating reactions in nearly all cells of the body. A part of this effect is attributed to increase in activity of many enzymes. Additionally, protein synthesis is affected by the thyroid hormones (121,122). [Pg.386]

Cells make use of many different types of membranes. All cells have a cytoplasmic membrane, or plasma membrane, that functions (in part) to separate the cytoplasm from the surroundings. In the early days of biochemistry, the plasma membrane was not accorded many functions other than this one of partition. We now know that the plasma membrane is also responsible for (1) the exclusion of certain toxic ions and molecules from the cell, (2) the accumulation of cell nutrients, and (3) energy transduction. It functions in (4) cell locomotion, (5) reproduction, (6) signal transduction processes, and (7) interactions with molecules or other cells in the vicinity. [Pg.260]

Cramer, W. A., and Kn2iff, D. B., 1990. Energy Transduction in Biological Membranes—A Textbook of Bioenergetics. New York Springer-Verlag, 545 pp. A textbook on bioenergetics by two prominent workers in photosyn diesis. [Pg.741]

Markin, V S. Thermodynamics of Membrane Energy Transduction in an Oscillating Field 24... [Pg.606]

Williams, R.J.P (1978). The multifarious couplings of energy transduction. Biochim. Biophys. Acta 505, 1. ... [Pg.154]

Eisenberg, E. Hill, T.L. (1985). Muscle contraction and free energy transduction in biological systems. Science 227,999-1006. [Pg.235]

Harada, Y., Sakurada, K., Aoki, T., Thomas, D.D., Yanagida, T. (1990). Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216,49-68. [Pg.236]

B. Perman, V. Srajer, Z. Ren, T. Teng, C. Pradervand, T. Ursby, D. Bourgeois, F. Schotte, M. Wulff, R. Kort, K. HeUingwerf, and K. Moffat, Energy transduction on the nanosecond time scale early structural events in a xanthopsin photocycle. Science 279, 1946-1950 (1998). [Pg.284]

Lys [47,48] and the fluorescein-5-isothiocyanate (FITC) reactive site Lys [49,50], as well as a region between residue 157 and 300, which has been proposed as part of an energy transduction region [40,44]. [Pg.29]

Crompton, M., McGuinness, O. and Nazareth, W. (1992). The involvement of cyclosporin A binding proteins in regulating and uncoupling mitochondrial energy transduction. Biochim. Biophys. Acta. 1101, 214. [Pg.70]

Hosier JP, Eerguson-Miller S, Mills DA. 2006. Energy transduction Proton transfer through the respiratory complexes. Annu Rev Biochem 75 165. [Pg.689]

W. A. Cramer and D. B. Knaff, Energy Transduction in Biological Membranes. A Textbook of Bioenergetics, Springer-Verlag, New York, 1990, pp. 353—465. [Pg.761]

Gust, D., Moore, T.A., and Moore, A.L. (2001) Mimicking photosynthetic solar energy transduction. Accounts of Chemical Research, 34 (1), 40-48. [Pg.133]

In addition, the authors suggest that all such systems must have a semi-permeable active boundary (membrane), an energy transduction apparatus and (at least) two types of functionally interdependent macromolecular components (catalysts and records). Thus, the phenomenon of life requires not only individual self-replication and self-sustaining systems, but it also requires of such individual systems the ability to develop a characteristic, evolutionary dynamic and a historical collectivist organisation. [Pg.16]

Apart from individual sites, series of metal ion sites provide electron conduction paths, vital in energy transduction in all organisms and leading to proton transfer, and Mg2+ in chlorophyll is essential for light capture (see Section 4.17). [Pg.172]

We next focus on the use of fixed-site cofactors and coenzymes. We note that much of this coenzyme chemistry is now linked to very local two-electron chemistry (H, CH3", CH3CO-, -NH2,0 transfer) in enzymes. Additionally, one-electron changes of coenzymes, quinones, flavins and metal ions especially in membranes are used very much in very fast intermediates of twice the one-electron switches over considerable electron transfer distances. At certain points, the chains of catalysis revert to a two-electron reaction (see Figure 5.2), and the whole complex linkage of diffusion and carriers is part of energy transduction (see also proton transfer and Williams in Further Reading). There is a variety of additional coenzymes which are fixed and which we believe came later in evolution, and there are the very important metal ion cofactors which are separately considered below. [Pg.205]


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