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  • 1
    Electronic Resource
    Electronic Resource
    Mutational analysis of assembly and function of the iron-sulfur protein of the cytochromebc 1 complex inSaccharomyces cerevisiae (1993)
    Springer
    Journal of bioenergetics and biomembranes 25 (1993), S. 245-257 
    Details
    ISSN: 1573-6881
    Keywords: Rieske iron-sulfur protein, RIP1 ; Saccharomyces cerevisiae ; mitochondria ; bc 1 complex ; QCR9 ; iron-sulfur cluster, mitochondrial targeting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The iron-sulfur protein of the cytochromebc 1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochromec 1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochromeb-566 heme group. In order to catalyze this divergent transfer of two reducing equivalents from ubiquinol, the iron-sulfur protein must be structurally integrated into the cytochromebc 1 complex in a manner which facilitates electron transfer from the iron-sulfur cluster to cytochromec 1 and generates a strongly reducing ubisemiquinone anion radical which is proximal to theb-566 heme group. This radical must also be sequestered from spurious reactivities with oxygen and other high-potential oxidants. Experimental approaches are described which are aimed at understanding how the iron-sulfur protein is inserted into center P, and how the iron-sulfur cluster is inserted into the apoprotein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762586
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The three-subunit cytochromebc 1 complex ofParacoccus denitrificans. Its physiological function, structure, and mechanism of electron transfer and energy transduction (1991)
    Springer
    Journal of bioenergetics and biomembranes 23 (1991), S. 241-255 
    Details
    ISSN: 1573-6881
    Keywords: P. denitrificans ; bc 1 complex ; protonmotive Q cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The cytochromebc 1 complex purified fromP. denitrificans has the same electron-transfer and energy-transducing activities, is sensitive to the same electron-transfer inhibitors, and contains cytochromesb, c 1, iron-sulfur protein, and thermodynamically stable ubisemiquinone identical to the counterpart complexes from mitochondria. However, the bacterialbc 1 complex consists of only three proteins, the obligate electron-transfer proteins, while the mitochondrial complexes contain six or more supernumerary poly-peptides, which have no obvious electron-transfer function. TheP. denitrificans complex is a paradigm for thebc 1 complexes of all gram-negative bacteria. In addition, because of its simple polypeptide composition and apparently minimal damage during isolation, theP. denitrificans bc 1 complex is an ideal system in which to study structure-function relationships requisite to energy transduction linked to electron transfer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762220
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    Paper (German National Licenses)
    Fulltext
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