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

Archives of Biochemistry and Biophysics
Yong-Hak KimMyeong-Hee Yu

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 (E(550-535)) 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 micromol 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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Citations

May 3, 2012·Chembiochem : a European Journal of Chemical Biology·Jacques LuxJean-François Nicoud
Sep 30, 2018·Experimental & Molecular Medicine·Sehyun ChaeKyong Soo Park
Jun 27, 2019·Scientific Reports·William Palmer-BrownCormac D Murphy

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