Decolorization of malachite green by cytochrome c in the mitochondria of the fungus Cunninghamella elegansopen access
- Authors
- Kim, Yong-Hak; Lee ,Cheolju; Go, Hayoung; Konishi, Kyoko; Lee, Kangseok; Lau, Peter C. K.; Yu, Myeong-Hee
- Issue Date
- Feb-2010
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Malachite green; Leucomalachite green; Triphenylmethane dyes; Cytochrome c; Cunninghamella elegans
- Citation
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, v.494, no.2, pp 159 - 165
- Pages
- 7
- Journal Title
- ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Volume
- 494
- Number
- 2
- Start Page
- 159
- End Page
- 165
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/22611
- DOI
- 10.1016/j.abb.2009.11.027
- ISSN
- 0003-9861
1096-0384
- 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 mu mol 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. (C) 2009 Elsevier Inc. All rights reserved.
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