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  • 1
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The generation of ethylene from 1-aminocyclopropane-1-carboxylic acid (ACC) added to a cell-free preparation from etiolated pea (Pisum sativum L. cv. Alaska) epicotyls was found not to be due to a specific ACC oxidase or to oxygen radicals. Rather, endogenously produced H2O and manganese ions are coupled in a reaction sequence which produces ethylene from ACC. In a model system, H2O and Mn2+ converted ACC to ethylene under conditions similar to those in the pea preparation. Ultrafiltration of the pea preparation inhibited ethylene production, but it could be reconstituted either by adding an H2O2-generating system to the ultrafiltrate or Mn2+ to the retentate. H2O2-generating systems could reconstitute ethylene formation in a heat-inactivated cell-free sample while the loss of ability to produce ethylene upon dialysis of the pea preparation correlated with the loss of Mn2+ from the sample. Studies using cell-free preparations to investigate ethylene synthesis should take care to exclude the possible involvement of H2O2 and Mn2+.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 66 (1986), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 64 (1985), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cytokinin bioassay material from six sources (Amaranthus caudatus L.; Avena sativa L.; Cucumis sativus L.; Funaria hygrometrica Hedw.; Pisum sativum L., cv. Alaska and cv. Progress No. 9; Xanthium pensylvanicum Wallr.) was analyzed for cyanide-resistant oxygen consumption (alternative respiration) during the course of a response to benzyladenine (40 μM). In five of the six bioassay systems, the alternative pathway was found to be present but disengaged (ϱ=0) in the cytokinin-treated material while untreated controls continued to fully utilize the pathway (ϱ=1). The moss, Funaria hygrometrica, was the exception to this pattern, with the alternative pathway fully engaged in both treated and untreated protonemata throughout the period of cytokinin-induced bud formation. Respiration via the alternative pathway was not inhibited by benzyladenine in this latter tissue, although titrations with benzyladenine in carrot (Daucus carota L.) cell suspensions mimicked those obtained using salicylhydroxamic acid, an inhibitor of the alternative pathway. The dwarf pea, Progress No. 9, showed no response to cytokinin application in terms of increased ethylene production, and was also found to lack any capacity for the alternative pathway. Taken together, these results point to a role for the alternative pathway in responses of at least some plant tissues to cytokinins.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Plant molecular biology 19 (1992), S. 135-147 
    ISSN: 1573-5028
    Keywords: URF13 ; cytoplasmic male sterility ; T-toxin ; corn leaf blight ; pore-forming protein ; T-urf13 ; pathotoxin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-2048
    Keywords: Cytokinin and alternative respiration ; Respiration, alternative
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A disengagement of the cyanide-resistant, alternative respiratory pathway in soybean (Glycine max (L.) Merr.) callus tissue was observed prior to the start of deoxyisoflavone production stimulated by addition of the cytokinin benzyladenine. To test whether this loss of alternativepathway activity was part of the response to cytokinin, inhibitors of the alternative pathway were assayed for their ability to elicit cytokinin-like responses. Salicylhydroxamic acid (SHAM) was found to produce a deoxyisoflavone difference spectrum similar to that observed following treatment of the callus tissue with benzyladenine, while propyl gallate (PG) was without effect. Both SHAM and PG were further tested for cytokinin-like activity in other bioassays. In two anti-senescence bioassays using leaf tissue (of Avena sativa L. and Xanthium pensylvanicum Wallr.) and in the Cucumis sativus L. bioassay which measures stimulation of weight gain by excised cotyledons, both SHAM and PG were effective “cytokinins” at 1 mM and 0.1 mM, respectively. In two other bioassays (betacyanin formation in Amaranthus caudatus L. seedlings and the soybean-callus celldivision assay), SHAM appeared to be toxic. These results substantiate the suggestion that effects on the alternative pathway may play a role in some cytokinin responses and further raise the question of what should be considered a true cytokinin response.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 13 (1981), S. 171-179 
    ISSN: 1573-6881
    Keywords: Cytochrome oxidase ; baker's yeast ; submitochondrial particles ; cytochrome a ; EPR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Cytochrome oxidase purified from baker's yeast submitochondrial particles is found to exist in a partially reduced state in the resting enzyme. Studies utilizing optical and EPR spectroscopy indicate that the “inactive” fraction contains a reduced low-spin heme, cytochromea, possibly indicating a block of electron transfer from cytochromea to cytochromea 3. There is no apparent reduction of either the EPR-detectable copper or the species associated with the 830 nm band. Oxidative titrations of the resting-state yeast cytochrome oxidase indicate that the reduction potential of the species titrating is higher than that of ferricyanide. This “inactive” cytochrome oxidase is not the result of the isolation procedure, but seems to represent a species which is present in the intact yeast.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 437-445 
    ISSN: 1573-6881
    Keywords: Maize ; mitochondria ; cytoplasmic male sterility ; URF13 ; T-urf13 ; T-toxin ; pathogenesis ; pore-forming receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract URF13 is the product of a mitochondrial-encoded gene (T-urfl3) found only in maize plants containing the Texas male-sterile cytoplasm (cms-T), and it is thought to be responsible for both cytoplasmic male sterility and the susceptibility ofcms-T maize to the fungal pathogensBipolaris maydis race T andPhyllosticta maydis. Mitochondria isolated fromcms-T maize are uniquely sensitive to pathotoxins (T-toxin) produced by these fungi and to methomyl (a commercial insecticide). URF13 acts as a receptor that specifically binds T-toxin to produce hydrophilic pores in the inner mitochondrial membrane. When expressed inEscherichia coli cells, URF13 also forms hydrophilic pores in the plasma membrane if exposed to T-toxin or methomyl. Topological studies established that URF13 contains three membrane-spanning α-helices, two of which are amphipathic and can contribute to pore formation. Chemical crosslinking of URF13 was used to demonstrate the existence of URF13 oligomers incms-T mitochondria andE. coli cells. The ability of the carboxylate-specific reagent,N,N∼-dicyclohexycarbodiimide, to cross-link URF13 was used in conjunction with site-directed mutagenesis to establish that the URF13 tetramer has a central core consisting of a four-α-helical bundle which undergoes a conformational change after interaction with T-toxin or methomyl. Overall, the experimental evidence indicates that URF13 functions as a ligand-gated, pore-forming T-toxin receptor incms-T mitochondria.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 27 (1995), S. 367-377 
    ISSN: 1573-6881
    Keywords: Alternative oxidase ; sequence homology ; hydroxo-bridged di-iron center proteins ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract A major characteristic of plant mitochondria is the presence of a cyanide-insensitive alternative oxidase which catalyzes the reduction of oxygen to water. Current information on the properties of the oxidase is reviewed. Conserved amino acid motifs have been identified which suggest the presence of a hydroxo-bridged di-iron center in the active site of the alternative oxidase. On the basis of sequence comparison with other di-iron center proteins, a structural model for the active site of the alternative oxidase has been developed that has strong similarity to that of methane monoxygenase. Evidence is presented to suggest that the alternative oxidase of plant mitochondria is the newest member of the class II group of di-iron center proteins.
    Type of Medium: Electronic Resource
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