EFFECT OF ANTIMYCIN-A ON CYTOCHROME-B561, CYTOCHROME-B566, AND THEIR RELATIONSHIP TO UBIQUINONE AND IRON-SULFUR CENTERS S-1 (+N-2) AND S-3
EFFECT OF ANTIMYCIN-A ON CYTOCHROME-B561, CYTOCHROME-B566, AND THEIR RELATIONSHIP TO UBIQUINONE AND IRON-SULFUR CENTERS S-1 (+N-2) AND S-3
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DOI：
10.1016/0003-9861(76)90333-7
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发表时间：
1976-01-01
影响因子：
3.9
通讯作者：
WILSON, DF
中科院分区：
文献类型：
--
作者：
ERECINSKA, M;WILSON, DF
研究了抗霉素A对细胞色素b561、b566、泛醌、铁-S中心S-1(+N-2)和S-3磷酸化位点Ⅱ呼吸链成分行为的影响。这些组分的表观还原电势(Em)值是根据它们在抗霉素A存在下的稳态还原水平计算出来的，假设与琥珀酸/富马酸对平衡，并与在氰化物存在下得到的值进行了比较。在需氧、抗霉素A抑制的稳定状态下，计算的细胞色素b561的Em值比氰化物抑制状态下的Em值多30 mV，细胞色素b566的Em值比氰化物抑制状态下的Em值多130 mV以上。泛醌中心和铁-S中心S-1(+N-2)和S-3在抗霉素A抑制的稳定状态下的EM值比氰化物抑制的稳定状态下的Em值大约负30 mV。抗霉素A的加入刺激鸽子线粒体产生H_2O_2和超氧阴离子。这些化合物的最高产率是在计算的细胞色素b561、泛醌和铁-S蛋白在氰化物存在下偏离它们的值最大的条件下。抗霉素A可能对磷酸化位点II的载体产生多重作用。
The effects of antimycin A on the behavior of the respiratory chain components at phosphorylation site II, cytochrome b561, b566, ubiquinone, Fe-S centers S-1 (+ N-2) and S-3, were examined. The apparent half-reduction potential (Em) values of these components were calculated from their steady-state reduction levels in the presence of antimycin A assuming equilibrium with the succinate/fumarate couple and compared with those obtained in the presence of cyanide. In the aerobic, antimycin A-inhibited steady state, the calculated Em value for cytochrome b561 became 30 mV more positive and that of cytochrome b566 more than 130 mV more positive than the respective values in the cyanide-inhibited state. The calculated Em values for ubiquinone and Fe-S centers S-1 (+N -2) and S-3 were approximately 30 mV more negative in the antimycin A-inhibited steady state than in the cyanide-inhibited steady state. Antimycin A addition stimulated production of H2O2 and superoxide anion by pigeon mitochondria. The highest rates of production of these compounds were under conditions where the shifts in the calculated Em values of cytochrome b561, ubiquinone, and Fe-S proteins away from their values in the presence of cyanide were maximal. Antimycin A may exert multiple effects on the carriers of phosphorylation site II.