By Valdur A. Saks, Renée Ventura-Clapier, Xavier Leverve, André Rossi, Michel Rigoulet
This quantity keeps 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 via booklet of the concentrated factor of Molecular and mobile are analyzed with admire to its molecular body structure and Biochemistry, quantity 133/134 and a booklet 'Cellular Bio sensible coupling to the adenine nucleotide translocase, as energetics: position of coupled creatine kinases' edited via V. Saks good as its participation, including the adenylate kinase and R. Ventura-Clapier and released via Kluwer Publishers, process, in intracellular strength move. the result of the Dordrecht -Boston. within the current quantity, use of quantitative reviews of creatine kinase poor transgenic mice are equipment of experiences of geared up metabolic platforms, akin to summarized and analyzed by utilizing mathematical types of mathematical modeling and Metabolic regulate research, for the compartmentalized strength move, therefore combining research of the issues of bioenergetics of the mobilephone is strong new equipment of the study. these kinds of effects, defined including presentation of latest experimental including the physiological and NMR facts at the cardiac effects. the next imperative difficulties of the mobile bio metabolic and mitochondrial responses to work-load alterations energetics are the focal point of the discussions: the mechanisms harmony to the concept that of metabolic networks of strength of rules of oxidative phosphorylation within the cells in vivo move and suggestions regulation.
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Additional resources for Bioenergetics of the Cell: Quantitative Aspects
Exp(39 . 118 . (7 -pHp »' k_3 = k03' ks = kGS . K;', k, = kos' k, = ko,' K;q . exp(--a' 02 . 39 . L1'P), k_,=ko,' exp(a· (1-0,)' 39 'L1'P) k03 = 200 R3 = 100 k05 = 1000 kG, = 200 k9 = k09 . K;q . exp(-p· 03 . 39 . L1'P), k9 = kG9 · exp(p, (1-03) . 39 . 03) kJO = kOJO . KJ'ri . exp(-y' 04 . 39 . 'P), kJO = kOJo ' exp(y' 4 ) ' 39 . 04  K;i = exp(39 . 17  K;i = exp(39 . 1) kJ2 = kGJ2 . K;r . exp(39 . 118 . 28  K;j = exp(-39 . 35) k JJ = kOJ3 . 01) kJ4 = kOJ4 . 21 nmole/mg pro ). 325 29 Table 5.
Moreover, the non-ohmic part was observed over a larger respiratory rate range in PUFA-deficient mitochondria. These data led us to exclude a single protonophoric effect (increase in ohmic leak), whereas a consequence of a change in non-ohmic proton leak might well be the case. Besides these effects in non-phosphorylating mitochondria, the main problem is the possible modification of the efficiency of oxidative phosphorylation since, as shown in Fig. 10, state 3 respiratory rate was unaffected while protonmotive force was largely decreased.
11 ~10-9 ~109 10-' 10- 7 150 200 250 300 350 L'>'P (mV) Fig. 7. 'P values in the minimal model, caused by 10- fold increase in the activities of steps 3 and 9, and I O-fold decrease in the activities of steps 4 and 7. Line I corresponds to the parameter values given in Table 3; line 2, k03 = 2000, k09 = 10000, k04 = 20, k07 = 100. actlVlty, V (see Eq. p- (the channel model) essentially exceeds that over Q. p - (the minimal model). This means that decrease in the succinate dehydrogenase activity will result in essential shift of the critical L1 'P to higher values in case of the channel model and insignificant changes of a dependence of the superoxide production rate on membrane potential in case of the minimal model (Figs 8a and 8b).
Bioenergetics of the Cell: Quantitative Aspects by Valdur A. Saks, Renée Ventura-Clapier, Xavier Leverve, André Rossi, Michel Rigoulet