Mitochondrial Cytochrome b560

  • Chang-An Yu
  • Linda Yu


Cytochrome b 560 the succinate-ubiquinone (Q) reductase region of the mitochondrial electron transfer chain was first reported by Davis et al. (1,2). In spite of the detection of cytochrome b 560 in various succinate -Q1 reductase (3,4), and Complex II (5–7) preparations, this cytochrome has often been regarded as a contaminant of the denatured cytochromes from ubiquinol-cytochrome c reductase because it is not reducible by succinate, and the spectra of dithionite reduced cytochrome b 560 in these preparations resembles the spectra of a mixture of denatured cytochromes b and c 1 of ubiquinol-cytochrome c reductase. Thus, the importance of this particular cytochrome b 560 has been slighted in the mammalian system. The participation of cytochrome b 560 in succinate dehydrogenase (SDH) of Bacillus subtilis (8) and Neurospora crassa (9), however, is well recognized. Recently, a substrate reducible cytochrome ¿558 was detected in muscle mitochondrial succinate-Q reductase from Ascaris suum (10). In this paper we report the properties of mitochondrial cytochrome b560 and its possible function in succinate oxidation and fumarate reduction.


Succinate Dehydrogenase Cytochrome B560 Midpoint Potential Succinate Oxidation Soret Absorption 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.











a protein complex that converts SDH into succinate-Q reductase


succinate dehydrogenase


sodium dodecylsulfate




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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Chang-An Yu
    • 1
  • Linda Yu
    • 1
  1. 1.Department of BiochemistryOklahoma State UniversityStillwaterUSA

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