Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Copper(I) coordination to olefin bonds in pyridine compounds containing di- and triisoprenyl substituent groups had been investigated. Results from Raman and optical spectroscopic studies in aqueous ethanolic solutions indicate formation of pi complexes of 1:1 stoichiometry, with K congruent to 10(4) M-1. Despite there being several potential Cu(I) ligation sites on the alkyl side chain, only a single olefin bond is coordinated. The data are consistent with a model comprising extensive folding of the isoprenyl groups in the polar medium, with Cu(I) binding occurring at the exposed olefin group on the terminal unit. Ligand-bridged binuclear ions were formed by simultaneous coordination of an oxidant metal ion, (NH3)5RuIII, to the pyridine ring nitrogen atoms and Cu(I) to side-chain olefin bonds. Electron-transfer pathways were determined by kinetic analysis; both rate laws and comparative redox rates for complexes containing a variety of 4-alkylpyridine ligands indicate reaction predominantly by intermolecular processes. No evidence for intramolecular electron transfer, i.e., from Cu(I) through the bridging ligand to the bound Ru(III) center, could be found. This result is discussed both in terms of its implications toward the existence of very similar pathways proposed for electron transfer between heme and copper redox sites in cytochrome oxidase and within the wider context of apparent differences in the fundamental mechanisms of electron transfer in biological particles and transition metal ions.
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PMID:Evaluation of the role of polyisoprenyl functional groups in biological electron transfer. Transition metal models. 42 28

The kinetics of electron transfer between cytochrome-c oxidase and ruthenium hexamine has been characterized using the native enzyme or its cyanide complex either solubilized by detergent (soluble cytochrome oxidase) or reconstituted into artificial phospholipid vesicles (cytochrome oxidase-containing vesicles). Ru(NH3)2+6 (Ru(II] reduces oxidized cytochrome a, following (by-and-large) bimolecular kinetics; the second order rate constant using the cyanide complex of the enzyme is 1.5 x 10(6) M-1 s-1, for the enzyme in detergent, and slightly higher for COV. In the case of COV the kinetics are not affected by the addition of ionophores. Upon mixing fully reduced cytochrome oxidase with oxygen (in the presence of excess reductants), the oxidation leading to the pulsed enzyme is followed by a steady state phase and (eventually) by complete re-reduction. When the concentrations of dioxygen and oxidase are sufficiently low (micromolar range), the time course of oxidation can be resolved by stopped flow at room temperature, yielding an apparent bimolecular rate constant of 5 x 10(7) M-1 s-1. After exhaustion of oxygen and end of steady state, re-reduction of the pulsed enzyme by the excess Ru(II) is observed; the concentration dependence shows that the rate of re-reduction is limited at 3 s-1 in detergent; this limiting value is assigned to the intramolecular electron transfer process from cytochrome a-Cua to the binuclear center. Using the reconstituted enzyme, the internal electron transfer step is sensitive to ionophores, increasing from 2-3 to 7-8 s-1 upon addition of valinomycin and carbonyl cyanide m-chlorophenylhydrazone. This finding indicates for the first time an effect of the electrochemical potential across the membrane on the internal electron transfer rate; the results are compared with expectations based on the hypothesis formulated by Brunori et al. (Brunori, M., Sarti, P., Colosimo, A., Antonini, G., Malatesta, F., Jones, M.G., and Wilson, M.T. (1985) EMBO J. 4, 2365-2368), and their bioenergetic relevance is discussed with reference to the proton pumping activity of the enzyme.
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PMID:Control of electron transfer by the electrochemical potential gradient in cytochrome-c oxidase reconstituted into phospholipid vesicles. 215 21

Cytochrome c oxidase can generate membrane potential in the absence of cytochrome c (e.g., in cytochrome c-deficient mitochondria or in proteoliposomes) with hexaammineruthenium as an artificial electron donor. Of several other redox mediators tested, phenazine methosulfate was found to be an efficient artificial substrate for membrane energization by cytochrome oxidase, whereas TMPD, DAD, DCPIP or ferrocyanide are virtually ineffective. The ability of Ru(NH3)6(2+) and phenazine methosulfate to support the generation of delta psi by cytochrome c-oxidase correlates with their effectiveness as electron donors to cytochrome a in the cyanide-inhibited membrane-bound enzyme.
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PMID:Hexaammineruthenium as an electron donor to mitochondrial cytochrome oxidase: membrane potential generation in the absence of cytochrome c. 300 96

When O2 was injected into an anaerobic suspension of valinomycin-treated rat liver mitochondria inhibited with rotenone, antimycin, and myxothiazol, a small amount of O2 (0.23-0.33 ng-atom of O/mg of protein) was reduced extremely rapidly (within the 2 s time-resolution of the oxygen electrode). The subsequent steady-state rate of flow of electrons to oxygen was very low [less than 3 nequiv. X s-1 X (g of mitochondrial protein)-1]. In the presence of valinomycin there was a rapid ejection of protons synchronous with the rapid phase of O2 consumption corresponding to 0.38-0.61 nequiv. of H+ X (mg of mitochondrial protein)-1. When valinomycin was replaced by carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) there was a rapid alkalification of the medium corresponding to 0.20-0.42 nequiv. of H+ X (mg of mitochondrial protein)-1. When 2 mM-Fe(CN)6(4-) was present to re-reduce endogenous cytochrome c, O2 consumption was still biphasic but the second phase of O2 consumption was very much more rapid [600 nequiv. X s-1 X (g of protein)-1], and resulted in the virtually complete consumption of the O2 in the pulse within 4 s. With 60 microM-Ru(NH3)6(2+) as reductant, O2 consumption was even faster [1200 nequiv. X s-1 X (g of protein)-1]. In a medium containing 150 mM-choline chloride with Ru(NH3)6(2+) as reductant, the proton per reducing equivalent stoichiometry (delta H+O/e-) was +0.95 in the presence of valinomycin and -0.94 in the presence of FCCP. In choline chloride medium containing Ru(NH3)6(2+) and valinomycin, there was an uptake of K+ ions corresponding to 1.86 K+/e-. It is concluded that nearly 1 proton is translocated outwards through cytochrome oxidase per oxidizing equivalent injected in this medium. In low ionic strength sucrose-based medium, with Ru(NH3)6(2+) as reductant, delta H+O/e- was 1.05 in the presence of valinomycin, and -0.71 in the presence of FCCP. It is concluded that the translocation of protons is accompanied by net acid production in this medium.
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PMID:Proton translocation by cytochrome oxidase in (antimycin + myxothiazol)-treated rat liver mitochondria using ferrocyanide or hexammineruthenium as electron donor. 302 18

When the calcium-transport inhibitor, ruthenium red, is chromatographed on a cation exchange resin, it yields a number of colored fractions and a colorless component that absorbs in the ultraviolet. The electron transfer activity previously ascribed to ruthenium red (Schwerzmann, K., Gazzotti, P., and Carafoli, E. (1976) Biochem. Biophys. Res. Commun. 69, 812) fractionates exclusively with the UV-absorbing material. On the basis of spectral, physical, and activity studies, we have identified this compound as Ru(NH3)62+/3+. It is shown that Ru(NH3)62+/3+ is an efficient electron donor directly to cytochrome oxidase, without mediation by cytochrome c. The steady state kinetics of electron transfer from Ru(NH3)62+ to purified oxidase resembles that of cytochrome c, showing a biphasic pattern but higher apparent Km values (Km1 = 8 microM, Km2 = 88 microM). Under conditions that favor tight binding to the oxidase, cytochrome c acts as a competitive inhibitor of Ru(NH3)62+, indicating that the two electron donors interact with cytochrome oxidase at the same site(s). The efficiency of Ru(NH3)62+ as an electron mediator to cytochrome aa3 and the similarity of its kinetic behavior to that of cytochrome c, make it a potentially valuable tool for investigating the mechanism of energy conservation in the terminal segment of the mitochondrial respiratory chain.
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PMID:An effective electron donor to cytochrome oxidase. Purification, identification, and kinetic characterization of a contaminant of ruthenium red, hexaamineruthenium II/III. 616 83

Initial steps of the Azotobacter vinelandii respiratory chain have been studied on the inside-out subcellular vesicles. Two NADH:ubiquinone oxidoreductases were revealed: (i) proton-motive, capsaicin-sensitive and oxidizing dNADH as well as NADH enzyme and (ii) enzyme non-coupled to the energy conservation, capsaicin-resistant and oxidizing only NADH. The level of the oxidoreductases strongly depends upon [O2] and [NH3] in the growth medium. Increase in [O2] results in lowering of the coupled-enzyme level and in rise of the non-coupled one. Exclusion of NH3 from the growth medium increases the level of the non-coupled enzyme whereas that of the coupled enzyme remains constant. The O2-linked control of NADH:ubiquinone oxidoreductases requires CydR, a Fnr-like regulatory protein. Summarizing the above observations with those made in this group on the terminal steps of the A. vinelandii respiratory chains, one can assume that the respiratory protection of nitrogenase could be carried out by co-operation of the non-coupled NADH:ubiquinone oxidoreductase and the "partially coupled" quinoloxidase of the bd-type. Efficiency of this chain seems to be five-fold lower than that of the usual proton-motive chain (the coupled NADH:ubiquinone oxidoreductase, the Q-cycle and cytochrome oxidase of the o-type) which is also present in A. vinelandii and operates at low [O2].
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PMID:Two NADH:ubiquinone oxidoreductases of Azotobacter vinelandii and their role in the respiratory protection. 950 87