Bioenergetics of the Cell: Quantitative Aspects by Valdur A. Saks, Renée Ventura-Clapier, Xavier Leverve, André

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By Valdur A. Saks, Renée Ventura-Clapier, Xavier Leverve, André Rossi, Michel Rigoulet

This quantity maintains the dialogue of the issues of in vivo and in vitro. The lately solved X-ray constitution of the mitochondrial creatine kinase and its molecular biology mobile bioenergetics - the culture we began in 1994 by means of ebook of the concentrated factor of Molecular and mobile are analyzed with appreciate to its molecular body structure and Biochemistry, quantity 133/134 and a booklet 'Cellular Bio­ sensible coupling to the adenine nucleotide translocase, as energetics: function of coupled creatine kinases' edited through V. Saks good as its participation, including the adenylate kinase and R. Ventura-Clapier and released through Kluwer Publishers, method, in intracellular power move. the result of the Dordrecht -Boston. within the current quantity, use of quantitative experiences of creatine kinase poor transgenic mice are equipment of reports of geared up metabolic platforms, reminiscent of summarized and analyzed by utilizing mathematical versions of mathematical modeling and Metabolic keep an eye on research, for the compartmentalized strength move, hence combining research of the issues of bioenergetics of the phone is strong new tools of the learn. these kinds of effects, defined including presentation of recent experimental including the physiological and NMR facts at the cardiac effects. the next important difficulties of the mobile bio­ metabolic and mitochondrial responses to work-load adjustments energetics are the point of interest of the discussions: the mechanisms harmony to the idea that of metabolic networks of strength of law of oxidative phosphorylation within the cells in vivo move and suggestions regulation.

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When considering the mechanism of the proton transport involved in chemiosmotic energy transduction, two different models have been proposed: a direct coupling, initially introduced by Mitchell [47], in which translocated protons 37 INTERNAL EXTERNAL -nE _ _ _ _ _ _ _ _ _ _ E-n H n E* Fig. 1. Six-state model of a proton pump as proposed by D. Pietrobon and R. Caplan [45]. E is an enzyme bearing n proton binding sites accessible either to the internal medium or to the external medium. The chemical reaction S (substrates) P (products) induces a conformational change in E to E *, this transition leading to a change in the accessibility of the bound protons (from the internal to the external media).

Exp(-~ . 8, . 39 . 5 k7 = k07 . K;"' exp(-y· 83 . 39 . 5 kg = k08 . K~q . exp(39 . 118 . 28 [3] K~q = exp(-39 . 035) k, = k09 . K;q, k9 = k09 k09 = 1000 K~ci = exp(39 . 0 I) k lo = kOlo . 12) K;q = exp(39 . 01 nmole/mgpr. 21 nmole/mg pro [28]). 325. Thus, at high membrane potentials, the electron transport from heme b l to bh is heavily suppressed and the bypassing flux of 0'2- production increases dramatically (cf. Fig. 3). 1600 1400 (f) z 1200 0 i= <{ 0:: IZ 1000 2 W o· z 800 0 0 ll.. 600 <{ 400 0 0 i= 0:: 200 0 0 50 100 150 200 250 300 6'1' (mV) Fig.

At similar magnitudes of parameters a critical increase in 0'2- production was observed at lower A'll for the channel, than for the minimal model (Fig. 2). e. at the same fixed concentrations of (QH2) p , Qp , Q n, Q. n-, pHp and the same (fixed) ratio of reduced and oxidized forms of FeSnJ" Figure 6 shows how the relative steady-state rate of transmembrane transfer of electron by cytochrome b depends on A'll. One can see that the electron transfer is suppressed at lower A'll values for the channel than for the minimal model.

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