The respiratory chain and proton electrochemical gradient in the alkalophile Bacillus pasteurii [proceedings].
نویسندگان
چکیده
It is also noteworthy that the maximum phosphorylation potential that may be generated by the vesicles (approx. 53.8kJ/mol) (Kell et al., 1978~) was not altered when the rate of NADH oxidation was inhibited by up to 60 %. The corollary of this result is that if Ap is poised at equilibrium with the phosphorylation potential then, as the phosphorylation potential does not decline when NADH oxidation is inhibited, our finding that Ap is not decreased on addition of rotenone is to be expected. The data presented above show that the resistance (or, more likely, the capacitance) of the P. denitrificans membrane must be variable. Both these data, and those of other workers (Casadio et al., 1978; Kupriyanov & Pobochin, 1978) would seem to point to the need to consider more localized factors in biomembrane energy-transduction processes. In this regard it may be profitable to utilize membrane models containing 3 capacitors in series (e.g. Andersen et al., 1978; cf. Bockris & Reddy, 1970).
منابع مشابه
Ammonium/urea-dependent generation of a proton electrochemical potential and synthesis of ATP in Bacillus pasteurii.
The influence of ammonium and urea on the components of the proton electrochemical potential (delta p) and de novo synthesis of ATP was studied with Bacillus pasteurii ATCC 11859. In washed cells grown at high urea concentrations, a delta p of -56 +/- 29 mV, consisting of a membrane potential (delta psi) of -228 +/- 19 mV and of a transmembrane pH gradient (delta pH) equivalent to 172 +/- 38 mV...
متن کاملDirect observation of protonation reactions during the catalytic cycle of cytochrome c oxidase.
Cytochrome c oxidase, the terminal protein in the respiratory chain, converts oxygen into water and helps generate the electrochemical gradient used in the synthesis of ATP. The catalytic action of cytochrome c oxidase involves electron transfer, proton transfer, and O2 reduction. These events trigger specific molecular changes at the active site, which, in turn, influence changes throughout th...
متن کاملInitiation of the proton pump of cytochrome c oxidase.
Cytochrome c oxidase is the terminal enzyme of the respiratory chain that is responsible for biological energy conversion in mitochondria and aerobic bacteria. The membrane-bound enzyme converts free energy from oxygen reduction to an electrochemical proton gradient by functioning as a redox-coupled proton pump. Although the 3D structure and functional studies have revealed proton conducting pa...
متن کاملKinetic models of redox-coupled proton pumping.
Cytochrome c oxidase, the terminal enzyme of the respiratory chain, pumps protons across the inner mitochondrial membrane against an opposing electrochemical gradient by reducing oxygen to water. To explore the fundamental mechanisms of such redox-coupled proton pumps, we develop kinetic models at the single-molecule level consistent with basic physical principles. We demonstrate that pumping a...
متن کاملProton-coupled electron transfer and the role of water molecules in proton pumping by cytochrome c oxidase.
Molecular oxygen acts as the terminal electron sink in the respiratory chains of aerobic organisms. Cytochrome c oxidase in the inner membrane of mitochondria and the plasma membrane of bacteria catalyzes the reduction of oxygen to water, and couples the free energy of the reaction to proton pumping across the membrane. The proton-pumping activity contributes to the proton electrochemical gradi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biochemical Society transactions
دوره 6 6 شماره
صفحات -
تاریخ انتشار 1978