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Gene Review

CYTB  -  cytochrome b

Sus scrofa

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High impact information on CYTB


Biological context of CYTB

  • Nucleotide sequences of the control (27 haplotypes) and cytochrome b (cyt-b) regions (19 haplotypes) were determined from 59 Japanese wild boars, 13 Ryukyu wild boars and 22 other boars and pigs [6].
  • It was concluded that the appearance of the plateau between the two reduction phases of Q and b is caused by the rapid delivery of electrons to the high-potential components of the respiratory chain as envisaged in the Q cycle; the unexpected n value for cytochrome b suggests a concerted reduction by QH2 of two species of cytochromes b-562 [7].

Anatomical context of CYTB


Associations of CYTB with chemical compounds


Other interactions of CYTB

  • These results are consistent with the postulated role of cytochrome b in O2.-formation by neutrophil NADPH oxidase, but raise doubts about the participation of flavoproteins in this enzyme activity [5].


  1. Superoxide-producing cytochrome b. Enzymatic and electron paramagnetic resonance properties of cytochrome b558 purified from neutrophils. Isogai, Y., Iizuka, T., Makino, R., Iyanagi, T., Orii, Y. J. Biol. Chem. (1993) [Pubmed]
  2. The electron transport chain of serotonin-dense granules of platelets. Johnson, R.G., Scarpa, A. J. Biol. Chem. (1981) [Pubmed]
  3. Mechanism of the superoxide-producing oxidase of neutrophils. O2 is necessary for the fast reduction of cytochrome b-245 by NADPH. Cross, A.R., Parkinson, J.F., Jones, O.T. Biochem. J. (1985) [Pubmed]
  4. The superoxide-generating oxidase of leucocytes. NADPH-dependent reduction of flavin and cytochrome b in solubilized preparations. Cross, A.R., Parkinson, J.F., Jones, O.T. Biochem. J. (1984) [Pubmed]
  5. Composition of partially purified NADPH oxidase from pig neutrophils. Bellavite, P., Jones, O.T., Cross, A.R., Papini, E., Rossi, F. Biochem. J. (1984) [Pubmed]
  6. Genetic relationship and distribution of the Japanese wild boar (Sus scrofa leucomystax) and Ryukyu wild boar (Sus scrofa riukiuanus) analysed by mitochondrial DNA. Watanobe, T., Okumura, N., Ishiguro, N., Nakano, M., Matsui, A., Sahara, M., Komatsu, M. Mol. Ecol. (1999) [Pubmed]
  7. Rapid redox equilibrium between the mitochondrial Q pool and cytochrome b during triphasic reduction of cytochrome b by succinate. Chen, M., Zhu, Q.S. Biochim. Biophys. Acta (1986) [Pubmed]
  8. Phagocytosis of brushite crystals by pig neutrophils. Higson, F.K., Jones, O.T. Ann. Rheum. Dis. (1985) [Pubmed]
  9. Is cytochrome b558 translocated into the plasma membrane from granules during the activation of neutrophils? Yamaguchi, T., Kaneda, M., Kakinuma, K. J. Biochem. (1986) [Pubmed]
  10. The triphasic reduction of cytochrome b in the succinate-cytochrome c reductase. Jin, Y.Z., Tang, H.L., Li, S.L., Tsou, C.L. Biochim. Biophys. Acta (1981) [Pubmed]
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