Dicyclohexylcarbodiimide inhibits proton pumping in ubiquinol:cytochrome c oxidoreductase of Rhodobacter sphaeroides and binds to aspartate-187 of cytochrome b.
Dicyclohexylcarbodiimide inhibits proton pumping in ubiquinol:cytochrome c oxidoreductase of Rhodobacter sphaeroides and binds to aspartate-187 of cytochrome b.
复制标题
Dicyclohexylcarbodiimide 抑制泛醇中的质子泵：球形红杆菌的细胞色素 c 氧化还原酶，并与细胞色素 b 的天冬氨酸 187 结合。
DOI：
10.1006/abbi.1998.0590
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发表时间：
1998
影响因子：
3.9
通讯作者：
Beattie,DS
中科院分区：
文献类型：
--
作者：
Wang,Y;Obungu,V;Beattie,DS
In recent studies we reported that dicyclohexylcarbodiimide (DCCD) inhibited proton translocation in ubiquinol:cytochrome c oxidoreductase (cytochrome bc1complex) from yeast mitochondria where it was bound to aspartate-160 of cytochrome b. In the current study, we report that DCCD and its fluorescent analogue,N-cyclohexyl-N′-[4-(dimethylamino)naphthyl]carbodiimide (NCD-4), inhibit 50–60% proton pumping in the cytochrome bc1complex of the bacteriumRhodobacter sphaeroideswith a 20% inhibition of electron transfer activity. Radioactive DCCD is bound exclusively to cytochrome b at aspartate-187, which is located at the C-terminal region of the CD loop connecting membrane-spanning helices C and D of cytochrome b. Fluorescent studies with NCD-4 revealed that aspartate-187 is located in a mildly hydrophobic pocket in the bc1complex at a distance of 2–3 Å from the surface of the membrane.
