ATP synthesis in mitochondria

Hatefi, Youssef

doi:10.1111/j.1432-1033.1993.tb18431.x

Cited by 76 publications

(44 citation statements)

References 104 publications

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“…Moreover, it has been demonstrated that expression of a plasmid bearing the genes encoding the ␣, ␤, and ␥ subunits of TF 1 in an unc Ϫ strain of Escherichia coli leads to overproduction of the assembled ␣ 3 ␤ 3 ␥ complex, which can be purified in high yield (9). For these reasons, the wild-type and mutant ␣ 3 ␤ 3 ␥ complexes are valuable tools for examining structure-function relationships in F 1 -ATPases.…”

mentioning

confidence: 99%

“…When separated from F 0 as a soluble complex, F 1 is composed of five different subunits in a stoichiometry of ␣ 3 ␤ 3 ␥␦⑀ and functions as an ATPase (2). The ␣ 3 ␤ 3 , ␣ 3 ␤ 3 ␥, and ␣ 3 ␤ 3 ␦ subcomplexes reconstituted from the isolated subunits of TF 1 1 are active as ATPases (3)(4)(5)(6). Both the ␣ 3 ␤ 3 and ␣ 3 ␤ 3 ␦ subcomplexes differ from TF 1 in that they are less specific for divalent cations and are insensitive to inhibition by azide (4,5).…”

mentioning

confidence: 99%

“…F 0 F 1 -ATP synthases found in energy-transducing membranes couple ATP synthesis and hydrolysis to proton electrochemical gradients (1). They are composed of an integral membrane protein complex, F 0 , which mediates proton conduction, and a peripheral membrane protein complex, F 1 , which bears the catalytic sites.…”

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confidence: 99%

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The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover

Jault

Dou

Grodsky

et al. 1996

Journal of Biological Chemistry

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The hydrolytic properties of the mutant ␣ 3 (␤T165S) 3 ␥ and wild-type ␣ 3 ␤ 3 ␥ subcomplexes of TF 1 have been compared. Whereas the wild-type complex hydrolyzes 50 M ATP in three kinetic phases, the mutant complex hydrolyzes 50 M ATP with a linear rate. After incubation with a slight excess of ADP in the presence of Mg 2؉ , the wild-type complex hydrolyzes 2 mM ATP with a long lag. In contrast, prior incubation of the mutant complex under these conditions does not affect the kinetics of ATP hydrolysis. The ATPase activity of the wild-type complex is stimulated 4-fold by 0.1% lauryl dimethylamine oxide, whereas this concentration of lauryl dimethylamine oxide inhibits the mutant complex by 25%. Compared with the wild-type complex, the activity of the mutant complex is much less sensitive to turnoverdependent inhibition by azide. This comparison suggests that the mutant complex does not entrap substantial inhibitory MgADP in a catalytic site during turnover, which is supported by the following observations. ATP hydrolysis catalyzed by the wild-type complex is progressively inhibited by increasing concentrations of Mg 2؉ in the assay medium, whereas the mutant complex is insensitive to increasing concentrations of Mg

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The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover

Jault

Dou

Grodsky

et al. 1996

Journal of Biological Chemistry

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“…In living cells, synthesis of ATP from ADP and inorganic phosphate is catalyzed by the ATP synthase complex in the final step of oxidative phosphorylation or photosynthesis [1]. Historically, the basic architectural principles of the mitochondrial ATP synthase, which consists of catalytic sector F 1 and membrane sector Fo, connected by the central and peripheral stalks, have been established in the course of the studies aimed at resolution and reconstitution of oxidative phosphorylation or its partial reactions, using membrane fragments derived from bovine heart mitochondria [2].…”

Section: Introductionmentioning

confidence: 99%

The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B

Belogrudov

2008

Archives of Biochemistry and Biophysics

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Treatment of the recombinant bovine factor B with trypsin yielded a fragment (amino acid residues 62-175) devoid of coupling activity. Removal of the N-terminal Trp2-Gly3-Trp4 peptide resulted in a significant loss of coupling activity in the FB ΔW 2 -W 4 deletion mutant. Sucrose density gradient centrifugation demonstrated co-sedimentation of recombinant factor B with the ADP/ATP carrier, which is present in preparations of H + -translocating F O F 1 -ATPase, but not in preparations of complex V. The N-terminally truncated factor B mutant FB ΔW 2 -W 4 did not co-sediment with the ADP/ATP carrier. Recombinant factor B co-sedimented with partially purified membrane sector F O , extracted from F 1 -stripped bovine submitochondrial particles with n-dodecyl-β-D-maltoside. Factor B inhibited the passive proton conductance catalyzed by F O reconstituted into asolectin liposomes. A factor B mutant, bearing a photoreactive unnatural amino acid pbenzoyl-L-phenyalalanine (pBpa) substituted for Trp2, cross-linked with F O subunits e and g as well as the ADP/ATP carrier. These results suggest that the N-terminal domain and, in particular, the proximal N-terminal amino acids are important for the coupling activity and protein-protein interactions of bovine factor B.

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“…Since they produce ATP for the cells, any damage to their activity induced by toxic compounds may affect the entire organism (Chance and Williams, Chemosphere 52 (2003) [1115][1116][1117][1118][1119][1120][1121][1122][1123] www.elsevier.com/locate/chemosphere 1955; Slater, 1967;Van Dam and Wiechmann, 1979;Mitchell, 1979;Hatefi, 1993). Therefore, mitochondria are good predictors for acute toxicity in solution as shown by Moreno and Madeira (1991), Shannon et al (1991), Jeevaratnam and Vidya (1994), Bragadin et al (1998), da Silva et al (1998 and Bragadin et al (1999a,b).…”

Section: Introductionmentioning

confidence: 99%

Frozen mitochondria as rapid water quality bioassay

Iero¹,

Manente²,

Perin³

et al. 2003

Chemosphere

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A rapid and relatively low cost bioassay, usable in routine screening water test has been developed modifying the beef heart mitochondria test. In our experiments, mitochondria (FM22) were frozen at )22°C, instead of )80°C (FM80), and their applicability and sensitivity was verified. The oxygen consumption was measured by a Clark electrode that was interfaced to a PC to collect test analysis data. Blank tests were carried out to verify the oxygen consumption linear fitting. Toxicity tests were performed using pure organic and inorganic compounds, such to verify the FM22 sensitivity. A piecewise regression, through an Excel â Macro, identified the break-point in the oxygen consumption and calculated the toxicity. The IC 50 s of the tested compounds were calculated and ranged from 0.123 to 0.173 mg/l for heavy metals (Cd, Cr, Cu, Ni, Pb and Zn) and from 0.572 to 10.545 mg/l for organics (benzene, DMSO, DDE, endrin, dichloromethane, chlorobenzene, 1,2-dichlorobenzene and 1,3-dichlorobenzene). Water effluent samples were then tested. The FM22 gave different toxic reactions to them. Water samples were characterised for heavy metals. The FM22 bioassay had a higher sensitivity than the FM80 and a high reproducibility in the toxicity test with pure compounds. The FM22 test was a good predictor of toxicity for water samples; the bioassay is easy, low cost and rapid, then usable for routine tests.

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ATP synthesis in mitochondria

Cited by 76 publications

References 104 publications

The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover

The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover

The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B

Frozen mitochondria as rapid water quality bioassay

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