Decolorization of malachite green by cytochrome c in the mitochondria of the fungus Cunninghamella elegans
- Decolorization of malachite green by cytochrome c in the mitochondria of the fungus Cunninghamella elegans
- 김용학; 이철주; 고하영; Kyoko Konishi; 이강석; 유명희
- Malachite green; Leucomalachite green; Triphenylmethane dyes; Cytochrome c; Cunninghamella elegans
- Issue Date
- Archives of biochemistry and biophysics
- VOL 494, NO 2, 159-165
- We 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.
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