Y. Mukohata, T. Yagi, Y. Sugiyama, Akemi Matsuno, M. Higashida
{"title":"Regulation of electron transport in isolated chloroplasts by sequential binding of adenine nucleotides to the coupling factor protein","authors":"Y. Mukohata, T. Yagi, Y. Sugiyama, Akemi Matsuno, M. Higashida","doi":"10.1007/BF01516403","DOIUrl":"https://doi.org/10.1007/BF01516403","url":null,"abstract":"","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"91-102"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01516403","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51711054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Electron transport coupled to quasi-arsenylation in isolated chloroplasts","authors":"Y. Mukohata, T. Yagi","doi":"10.1007/BF01516405","DOIUrl":"https://doi.org/10.1007/BF01516405","url":null,"abstract":"","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"111-121"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01516405","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51711065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Inhibition and uncoupling of the ADP-regulated electron transport in isolated chloroplasts","authors":"Y. Mukohata, T. Yagi, Y. Sugiyama","doi":"10.1007/BF01516404","DOIUrl":"https://doi.org/10.1007/BF01516404","url":null,"abstract":"","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"103-109"},"PeriodicalIF":0.0,"publicationDate":"1975-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01516404","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51711056","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The possible role of palmitoyl-CoA in the regulation of the adenine nucleotides transport in mitochondria under different metabolic states. I. Comparison of liver mitochondria from starved and fed rats.","authors":"A V Panov, Y M Konstantinov, V V Lyakhovich","doi":"10.1007/BF01558428","DOIUrl":"https://doi.org/10.1007/BF01558428","url":null,"abstract":"<p><p>It has been shown that KM values for ADP when rat liver mitochondria oxidized succinate were strictly dependent on the values of the respiratory control ratios. The Ki values for palmitoyl-CoA inhibition of the ADP-stimulated succinate oxidation and the inhibition of the uncoupler-stimulated ATPase activity were equal to 0.5 muM. Mitochondria from livers of starved rats showed 30% inhibition of the state 3 respiratory rate (compared to the uncoupled respiratory rate) which was abolished by addition of carnitine. It was supposed that this inhibition was due to the influence of acyl-CoAs bound to the inner mitochondrial membrane on the adeninenucleotide translocase. Mitochondria from livers of fed rats showed a strong inhibition of succinate oxidation both in state 4 and state 3, although the rate of uncoupled respiration was normal. It was assumed that in this case the changes in mitochondrial behaviour was caused by the decrease in the concentration of ADP and ATP in the matrix space of mitochondria.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 2","pages":"75-85"},"PeriodicalIF":0.0,"publicationDate":"1975-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558428","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12362842","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Bound ATP in chloroplast membranes: formation and effect of different inhibitors on the labelling.","authors":"C Pflugshaupt, R Bachofen","doi":"10.1007/BF01558426","DOIUrl":"https://doi.org/10.1007/BF01558426","url":null,"abstract":"<p><p>Chloroplast membranes contain firmly bound nucleotides. Their synthesis seems not to be dependent on energy. The amount of labelled firmly bound ATP extracted from membranes after incubation in the light of the presence of 32Pi is only slightly affected by uncouplers such as desapidin and CCCP or energy transfer inhibitors as phlorizin at concentrations where steady state phosphorylation is completely abolished. With Dio-9 or NEM, however, the labelling of firmly bound ATP is lowered to a similar extent as the steady state phosphorylation. These effects can be explained assuming a direct modification of the coupling factor. The results of a two stage incubation experiment using a rapid filtration technique support our earlier hypothesis that the gammaP in the liberated ATP does not origin from the previously built phosphorylated intermediate.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 2","pages":"49-60"},"PeriodicalIF":0.0,"publicationDate":"1975-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558426","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11997530","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
B Griniuviene, V Chmieliauskaite, V Melvydas, P Dzheja, L Grinius
{"title":"Conversion of Escherichia coli cell-produced metabolic energy into electric form.","authors":"B Griniuviene, V Chmieliauskaite, V Melvydas, P Dzheja, L Grinius","doi":"10.1007/BF01558460","DOIUrl":"10.1007/BF01558460","url":null,"abstract":"<p><p>The formation of membrane potential in energized E. coli cells has been investigated by means of ionic penetrants. The fluxes of anions and cations in opposite directions have been observed: anions moved out and cations moved into the cells. The energy-linked uptake of cations was stoichiometrically coupled with the outflow of H+ ions from the cells. The value of a membrane potential in the energized cells calculated from a distribution of permanent cations was in the range of -140 mV (inside minus). The uptake of penetrating cations by deenergized cells has been observed following the non-enzymatic generation of a membrane potential. The influx of synthetic and natural (lactose) penetrants collapsed the non-enzymatic membrane potential. The effect of lactose was sensitive to N-ethyl maleimide. These results are in favour of the conception that in the energized E. coli cells an energy-linked H+-pump generates a membrane potential which is a driving force for the transport of synthetic and some natural penetrants.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"17-38"},"PeriodicalIF":0.0,"publicationDate":"1975-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11454703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Change of mitochondrial buffering capacity induced by propranolol.","authors":"J O Järvisalo","doi":"10.1007/BF01558461","DOIUrl":"https://doi.org/10.1007/BF01558461","url":null,"abstract":"<p><p>Propranolol is able to increase the amount of the titratable groups of mitochondrial membranes. This effect occurs with sonicated particles and with liposomes, too. The phenomenon is only seen in the presence of salt solutions, not in sucrose. Propranolol increases the fluorescence of anilino-naphthalene sulphonate (ANS) in mitochondrial suspensions. The increase is counteracted by increasing concentrations of potassium chloride. It is suggested that the increase of the titratable groups results from a decrease of the aggregation of the phospholipids of the membranes. At the same time the environment of the bound ANS molecules is more hydrophobic in sucrose than in potassium chloride. The amount of the buffering groups and the hydrophilicity are in direct and the amount of the buffering groups and the fluorescence of ANS in inverse correlation.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"39-48"},"PeriodicalIF":0.0,"publicationDate":"1975-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558461","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11454704","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Correlation of the effects of citric acid cycle metabolites on succinate oxidation by rat liver mitochondria and submitochondrial particles.","authors":"M Hillar, V Lott, B Lennox","doi":"10.1007/BF01558459","DOIUrl":"https://doi.org/10.1007/BF01558459","url":null,"abstract":"<p><p>1. Succinate dehydrogenase is inhibited by citrate and beta-hydroxy-butyrate in a complex manner, both in mitochondria and submitochondrial particles. Kinetics of inhibition in the particles points to a competitive component in the mechanism involved. 2. Pyruvate, alpha-ketoglutarate, malate, and glutamate stimulate oxidation of succinate by mitochondria. 3. Stimulation by alpha-ketoglutarate and glutamate is not influenced by the presence of rotenone. 4. Stimulation by pyruvate is higher in the absence of rotenone and increases significantly in the presence of K+ and valinomycin. Pyruvate supplies in mitochondria reducing equivalents for malate dehydrogenase operating in the reverse direction-reduction of oxaloacetate to malate. 5. Stimulation by malate is higher in the presence of rotenone.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"1-16"},"PeriodicalIF":0.0,"publicationDate":"1975-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558459","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12352847","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}