{"title":"Methods in membrane biology","authors":"E. Korn","doi":"10.1007/978-1-4757-5820-7","DOIUrl":"https://doi.org/10.1007/978-1-4757-5820-7","url":null,"abstract":"","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"7 1","pages":"87-88"},"PeriodicalIF":0.0,"publicationDate":"2013-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51030964","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":"Influence of surface potentials on the mitochondrial H+ pump and on lipid-phase transitions.","authors":"G Schäfer, G Rowohl-Quisthoudt","doi":"10.1007/BF01558629","DOIUrl":"https://doi.org/10.1007/BF01558629","url":null,"abstract":"<p><p>It has been shown that the surface potential of lipid membranes, as well as of mitochondria, can be shifted more positive by absorption of alkylbiguanides. Both phospholipid vesicles and natural membranes respond in an analogous way to this shift. Ion activities at the immediate membrane surface are influenced by sign and magnitude of the surface charge. Corresponding effects on ion transport and on fluorescence-probe binding can be observed. The mitochondrial H+ pump is inhibited when the surface charge is shifted more positive. In contrast,the absolute charge density determines the temperature of the ordered-fluid transition. The latter is increased by biguanides, suggesting that the membrane is rendered more rigid. The experiments make obvious that physical relations derived from model systems apply equally well to lipid-containing natural membranes.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 2","pages":"73-81"},"PeriodicalIF":0.0,"publicationDate":"1976-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558629","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11232258","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":"Coupling factors ATPases from photosynthetic bacteria.","authors":"B A Melandri, A B Melandri","doi":"10.1007/BF01558632","DOIUrl":"https://doi.org/10.1007/BF01558632","url":null,"abstract":"","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 2","pages":"109-19"},"PeriodicalIF":0.0,"publicationDate":"1976-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558632","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11353222","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":"Evidence for multiple sites of ferricyanide reduction in chloroplasts.","authors":"J Banaszak, R Barr, F L Crane","doi":"10.1007/BF01558630","DOIUrl":"https://doi.org/10.1007/BF01558630","url":null,"abstract":"<p><p>Various sites of ferricyanide reduction were studied in spinach chloroplasts. It was found that in the presence of dibromothymoquinone a fraction of ferricyanide reduction was dibromothymoquinone sensitive, implying that ferricyanide can be reduced by photosystem I as well as photosystem II. To separate ferricyanide reduction sites in photosystem II, orthophenanthroline and dichlorophenyl dimethylurea inhibitions were compared at various pHs. It was noted that at low pH ferricyanide reduction was not completely inhibited by orothophenanthroline. At high pH's, however, inhibition of ferricyanide reduction by orthophenanthroline was complete. It was found that varying concentration of orthophenanthroline at a constant pH showed different degrees of inhibition. In the study of ferricyanide reduction by photosystem II various treatments affecting plastocyanin were performed. It was found that Tween-20 or KCN treatments which inactivated plastocyanin did not completely inactivate ferricyanide reduction. These data support the conclusion that ferricyanide accepts electrons both before and after plastoquinone in photosystem II.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 2","pages":"83-92"},"PeriodicalIF":0.0,"publicationDate":"1976-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558630","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11232259","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":"Genetic analysis of mitochondrial biogenesis and function in Saccharomyces cerevisiae.","authors":"G Michaelis, M Somlo","doi":"10.1007/BF01558631","DOIUrl":"https://doi.org/10.1007/BF01558631","url":null,"abstract":"<p><p>Different mitochondrial mutants have been isolated that affect mitochondrial ribosome function. These mutants were used to establish most of the known methods and principles of mitochondrial genetics in yeast. Another class of mitochondrial mutants have been shown to affect mitochondrial ATPase and, more specifically, the \"membrane factor\" of mitochondrial ATPase. These mutants might be very useful in studying the energy-conserving function, and the interaction between the hydrophobic and hydrophylic parts, of the ATPase complex. New types of mitochondrial point mutations, concerning cytochrome a-a3 or b, will soon open up new fields of investigation. The biochemical and genetic analysis of numerous mutants belonging to that category and recently obtained [31] is being currently pursued in Tzagoloff's and Slonimski's laboratories.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 2","pages":"93-107"},"PeriodicalIF":0.0,"publicationDate":"1976-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01558631","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11353223","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":"Steroidogenesis in the zona glomerulosa of the adrenal coretx. I. Isolation and some properties of mitochondria from the zona glomerulosa of the bovine adrenal cortex.","authors":"T Wakabayashi, C Kurono, M Asano","doi":"10.1007/BF01559388","DOIUrl":"https://doi.org/10.1007/BF01559388","url":null,"abstract":"<p><p>Isolation procedures for mitochondria from the zona glomerulosa of the bovine adrenal cortex are described and the properties of the mitochondria thus prepared are compared with those isolated from the zona fasciculoreticularis. The cristal membranes of mitochondria in the zona glomerulosa in situ are tubular or tubulovesicular, whereas those of mitochondria in the zona fasciculoreticularis in situ are vesicular. When mitochondria are isolated from the former zone, they invariably showed the condensed configuration regardless of isolation media, whereas those isolated from the latter zone in an ST medium showed the orthodox configuration. When Ca2+ was added to mitochondria isolated either from the zona glomerulosa or the zona fasciculoreticularis in an STE medium in the condensed configuration, a transition from the condensed to the orthodox configuration tool place; the cristal membranes of mitochondria from the zona glomerulosa became tubular or tubulovesicular and those of mitochondria from the zona fasciculoreticularis became vesicular. Contaminations of mitrochondria of the zona glomerulosa with other cellular organelles were examined using various marker enzymes. There was no difference in cytochrome content between mitochondria of the two zones specified above. The coupling efficiency of mitochondria of the zona glomerulosa was found to be remarkably effected by temperature during the isolation procedures. Effects of various substrates, isolation media, and bovine serum albumin on the coupling efficiency of mitochondria of the zona glomerulosa are also described.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 1","pages":"27-53"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01559388","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12139510","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}
T Wakabayashi, C Kurono, M Asano, H Kimura, T Ozawa
{"title":"Steroidogenesis in the zona glomerulosa of the adrenal cortex. II. Distribution of cytochrome P-450 in the zona glomerulosa of the bovine adrenal cortex.","authors":"T Wakabayashi, C Kurono, M Asano, H Kimura, T Ozawa","doi":"10.1007/BF01559389","DOIUrl":"https://doi.org/10.1007/BF01559389","url":null,"abstract":"<p><p>Microsomes were obtained from the zona glomerulosa of the bovine adrenal cortex. Contamination of microsomes with other cellular organelles was examined using various marker enzymes and the electron microscope. Distribution of cytochrome P-450 in mitochondria and in microsomes was determined to be 0.73 and 0.32 nmol/mg protein, respectively. The CO difference spectrum was affected not only by the concentration of added deoxycholate but also by the incubation time after addition. Approximately 40-50% of cytochrome P-450 in the samples was converted to cytochrome P-420 within 20-30 sec of incubation with deoxycholate. The content of RNA, phospholipids, and cytochrome b5 in microsomes obtained from the zona glomerulosa is also evaluated in comparison to that in microsomes obtained from the zona fasciculoreticularis.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 1","pages":"55-71"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01559389","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12169697","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":"Charge transfer mediated by nigericin in black lipid membranes.","authors":"M Toro, C Gómez-Lojero, M Montal, S Estrada-O","doi":"10.1007/BF01559387","DOIUrl":"https://doi.org/10.1007/BF01559387","url":null,"abstract":"<p><p>Nigericin, in the concentration range (10(-6) M or higher) at which it uncouples intact mitochondria, was found to increase the conductance of black lipid membranes (BLM) by several orders of magnitude. The dependence of the membrane conductance on pH and K+ concentration suggests a mechanism for the transfer of charge mediated by this ionophore based on a mobile dimer with both nigericin molecules protonated and complexed with one K+. This charged complex accounts for the uncoupling effect observed in intact mitochondria.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 1","pages":"19-26"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01559387","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11232257","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}
I A Kozlov, A A Kondrashin, V A Kononenko, S T Metelsky
{"title":"Functional role of soluble mitochondrial ATPase subunits.","authors":"I A Kozlov, A A Kondrashin, V A Kononenko, S T Metelsky","doi":"10.1007/BF01559385","DOIUrl":"https://doi.org/10.1007/BF01559385","url":null,"abstract":"<p><p>A preparation of soluble mitochondrial ATPase (coupling factor F1) containing no gamma and delta minor subunits has been isolated. The minor-subunits-deficient F1 was found to be competent in ATP hydrolysis. However, it did not demonstrate a \"coupling\" effect in EDTA-submitochondrial particles. A portion of the ATPase activity of EDTA particles, stimulated by the minor-subunits-deficient F1, was insensitive to oligomycin. ATPase activity of Na+-particles was changed only slightly by this F1. It is suggested that gamma and delta subunits are necessary to form specific contacts between the F1 molecule and components of the mitochrondrial membrane.</p>","PeriodicalId":75989,"journal":{"name":"Journal of bioenergetics","volume":"8 1","pages":"1-7"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF01559385","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11353221","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}