The effects of carbodiimides on functions associated with the energy-conservation mechanism in beef heart sub-mitochondrial particles

Beechey, R. B.; Knight, I. G.

doi:10.1007/bf00743054

Cited by 6 publications

(2 citation statements)

References 29 publications

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“…To avoid this, a sample from BDH Chemicals was used and made up fresh every day. However, Beechey and Knight [39] stated that DCCD was stable in ethanol, contrary to our finding.…”

Section: Methodscontrasting

confidence: 99%

Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

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Brand²

1983

European Journal of Biochemistry

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We report here that N,N/i′‐dicyclohexylcarbodiimide (DCCD) decreases the H2e stoichiometry of the mytochrome bc1 complex from 308 ± 0.2 (10) to 201 ± 0.1 (8) but has only a minimal effect on the H2e ratio of cytochrome oxidase under the relatively mild condition used. The veffect on the bc1 complex connot be explained by uncoupling, by inhibition of electron transport or by selective mitochondrial damage. We conclude that DCCD is an inhibitor of proton translocation within ther bc1 complex. There are three possible explanation of this effect: (a) DCCD could alter the pathway of electron flow, (b) DCCD could prevent one of the proton translocation reations but not electrton transport, (c) DCCD could prevent the couduction of the translocated proton to the external phase.

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“…To avoid this, a sample from BDH Chemicals was used and made up fresh every day. However, Beechey and Knight [39] stated that DCCD was stable in ethanol, contrary to our finding.…”

Section: Methodscontrasting

confidence: 99%

Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Price¹,

Brand²

1983

European Journal of Biochemistry

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“…Whether DCCD affects the transhydrogenase more directly when this enzyme is coupled to electron transport or to the ATPase merits further study. However, it is of interest that the mammalian nonenergy-linked transhydrogenation also is unaffected by DCCD and related carbodiimides, but energy-linked activities are significantly inhibited (Roberton et al 1968;Beechey and Knight 1978).…”

Section: Discussionmentioning

confidence: 97%

Catalysis of NADH→NADP+ transhydrogenation by adult Hymenolepis diminuta mitochondria

Park

Fioravanti

2005

Parasitol Res

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Hymenolepis diminuta mitochondria catalyze nonenergy-linked and energy-linked NADH-->NADP(+) transhydrogenations, with the latter driven by electron-transport dependent NADH oxidation (electron transport-driven, ETD) or ATP hydrolysis (ATP-driven, ATPD). Using submitochondrial particles, NADH-->NADP(+) transhydrogenations were characterized further. ETD and ATPD reactions were enhanced by bovine serum albumin (BSA) and were inhibited by N,N'-dicyclohexylcarbodiimide (DCCD), carbonyl cyanide 3-chlorophenylhydrazone (CCCP), carbonyl cyanide 4-(trifluoromethoxy) phenylhydrazone (FCCP), and niclosamide. The nonenergy-linked reaction was unaffected by these additives. Except for DCCD inhibition of the ATPD reaction, BSA mitigated inhibitor effects on energy-linked activities. BSA enhanced NADH oxidase (but not ATPase) activity. Although DCCD inhibited NADH oxidase and ATPase, BSA only lessened oxidase inhibition. With protonophores, an increase in NADH oxidase (but not ATPase) activity was suggested. Oxidase inhibition by rotenone was unaffected by BSA. The ATP-hydrolyzed/NADPH-formed for the ATPD reaction was almost unity. A model for H. diminuta energy-linked transhydrogenation is presented.

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Conformational coupling in H+-pumps and ATP synthesis ? its analysis with anisotropic inhibitors of energy transduction in oxidative phosphorylation

Higuti

1984

Mol Cell Biochem

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The analysis of anisotropic inhibitor-induced phenomena in mitochondria revealed that two kinds of negative charges are generated near surface of the C-side of mitochondrial inner membranes in the energized state, on the redox complexes (I, III & IV) and F0, respectively, and that positively charged anisotropic inhibitors (AI+) inhibit energy transduction in oxidative phosphorylation by binding to these negative charges. Thus, AI+ have two different inhibition sites in oxidative phosphorylation, the redox complexes and F0. The membrane components generating the negative charges in energized mitochondria were examined by the technique of photoaffinity labeling with monoazide ethidium, which is an AI+. Results showed that monoazide ethidium specifically binds to two kinds of hydrophobic protein (of 8 K and 13 K daltons) of mitochondria energized with succinate, and these proteins were named chargerin I and II, respectively. Chargerin I and II, which may be components of the redox complexes and Fo, seem to generate the negative charges described above, and these may be essential for H+-pumps in the redox complexes and F1 X F0. AI+ seem to inhibit ATP synthesis by binding to negatively charged sites of chargerin I and II. Based on these findings and the salient results on energy-transducing membranes obtained recently in other laboratories, a conformational model of H+-pumps and ATP synthesis in mitochondria is proposed, which is also applicable to ATP synthesis in other energy-transducing membranes and ATP-linked active transport of ions.

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The effects of carbodiimides on functions associated with the energy-conservation mechanism in beef heart sub-mitochondrial particles

Cited by 6 publications

References 29 publications

Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Catalysis of NADH→NADP+ transhydrogenation by adult Hymenolepis diminuta mitochondria

Conformational coupling in H+-pumps and ATP synthesis ? its analysis with anisotropic inhibitors of energy transduction in oxidative phosphorylation

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The effects of carbodiimides on functions associated with the energy-conservation mechanism in beef heart sub-mitochondrial particles

Cited by 6 publications

References 29 publications

Chemical Modification of the Mitochodrial bc1 by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Chemical Modification of the Mitochodrial bc1 by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Catalysis of NADH→NADP+ transhydrogenation by adult Hymenolepis diminuta mitochondria

Conformational coupling in H+-pumps and ATP synthesis ? its analysis with anisotropic inhibitors of energy transduction in oxidative phosphorylation

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Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation

Chemical Modification of the Mitochodrial bc₁ by N,N′ ‐Dicyclohexylcarbodiimide Inhibits Proton Translocation