Decolorization of malachite green by cytochrome c in the mitochondria of the fungus Cunninghamella elegans |
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Authors: | Yong-Hak Kim Cheolju Lee Kyoko Konishi Peter C.K. Lau |
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Affiliation: | a Functional Proteomics Center, Korea Institute of Science and Technology, Seongbuk, Seoul 136-791, Republic of Korea b Life Sciences Division, Korea Institute of Science and Technology, Seongbuk, Seoul 136-791, Republic of Korea c Department of Life Science, Chung-Ang University, Dongjak-Gu, Seoul 156-756, Republic of Korea d Biotechnology Research Institute, National Research Council Canada, 6100 Royalmount Ave., Montreal, Quebec, Canada H4P 2R2 |
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Abstract: | 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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Keywords: | Malachite green Leucomalachite green Triphenylmethane dyes Cytochrome c Cunninghamella elegans |
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