Decolorization of malachite green by cytochrome c in the mitochondria of the fungus Cunninghamella elegans

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DOIResolve DOI: http://doi.org/10.1016/j.abb.2009.11.027
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TypeArticle
Journal titleArchives of Biochemistry and Biophysics
Volume494
Issue2
Pages159165; # of pages: 7
SubjectMalachite green; Leucomalachite green; Triphenylmethane dyes; Cytochrome c; Cunninghamella elegans
AbstractWe studied the decolorization of malachite green (MG) by the fungus Cunninghamella elegans. The mitochondrial activity for MG reduction was increased with a simultaneous increase of a 9-kDa protein, called CeCyt. The presence of cytochrome c in CeCyt protein was determined by optical absorbance spectroscopy with an extinction coefficient (E₅₅₀–₅₃₅) of 19.7 ± 6.3 mM-¹ cm-¹ and reduction potential of + 261 mV. When purified CeCyt was added into the mitochondria, the specific activity of CeCyt reached 440 ± 122 μmol min-¹ mg-¹ protein. The inhibition of MG reduction by stigmatellin, but not by antimycin A, indicated a possible linkage of CeCyt activity to the Qo site of the bc1 complex. The RT-PCR results showed tight regulation of the cecyt gene expression by reactive oxygen species. We suggest that CeCyt acts as a protein reductant for MG under oxidative stress in a stationary or secondary growth stage of this fungus.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Biotechnology Research Institute
Peer reviewedYes
NRC number50008
NPARC number14262109
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Record identifier6496d10b-f81e-44bd-b0b5-53afd32c457a
Record created2010-06-02
Record modified2016-05-09
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