Literature DB >> 2080921

Oxidation-reduction potentials of cytochromes in Ascaris muscle mitochondria: high-redox-potential cytochrome b558 in complex II (succinate-ubiquinone reductase).

S Takamiya1, K Kita, K Matsuura, R Furushima, H Oya.   

Abstract

Oxidation-reduction midpoint potentials (Ems) were determined at pH 7.0 for cytochromes in the anaerobic respiratory chain of Ascaris mitochondria by redox titration techniques. Cytochrome b558, which is associated with complex II that functions as fumarate reductase in the terminal step of the respiratory chain, was shown to have an Em of -34 mV in the isolated complex II and -54 mV in mitochondria. These values are much higher than the value of Ascaris cytochrome b558. In contrast, Ems of cytochromes C + C1 and cytochrome b559.5 were determined in situ to be 235 mV and 78 mV, respectively, which are comparable to those of their mammalian counterparts.

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Year:  1990        PMID: 2080921

Source DB:  PubMed          Journal:  Biochem Int        ISSN: 0158-5231


  2 in total

Review 1.  Expression and functional properties of fumarate reductase.

Authors:  J J Van Hellemond; A G Tielens
Journal:  Biochem J       Date:  1994-12-01       Impact factor: 3.857

2.  Unique structure of Ascaris suum b5-type cytochrome: an additional alpha-helix and positively charged residues on the surface domain interact with redox partners.

Authors:  Takehiro Yokota; Yoshitaka Nakajima; Fumiyuki Yamakura; Shigetoshi Sugio; Muneaki Hashimoto; Shinzaburo Takamiya
Journal:  Biochem J       Date:  2006-03-01       Impact factor: 3.857

  2 in total

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