Klingenberg M
Eur J Biochem. 1976 Jun 1;65(2):601-5. doi: 10.1111/j.1432-1033.1976.tb10377.x.
The reported studies are intended to clarify the binding state of ADP fixed to mitochondria under the influence of bongkrekate, and thus to discern between the affinity increase and reorientation mechanism proposed for the bongkrekate effect. (a) The composition of the intramitochondrial adenine nucleotide pool is not changed under the influence of bongkrekate with and without added nucleotides. (b) The added ADP and ATP fixed by bongkrekate can be identified as AMP, ADP and ATP in the same proportions as in the endogenous pool. (c) The bound nucleotides respond to oxidative phosphorylation or uncoupler stimulated dephosphorylation similar as endogenous nucleotides. It can be concluded that the ADP or ATP fixed under the influence of bongkrekate to the mitochondria are equilibrated with the intramitochondrial adenine nucleotide pool and are active in intramitochondrial phosphate transfer reactions. The results disagree with the affinity increase mechanism but support the reorientation mechanism which postulates that ADP and ATP are trapped in the mitochondria under the influence of bongkrekate in the same amount as there are carrier sites available outside before bongkrekate addition.
所报道的研究旨在阐明在邦克里酸影响下固定于线粒体的ADP的结合状态,从而区分针对邦克里酸效应提出的亲和力增加机制和重新定向机制。(a) 在添加或不添加核苷酸的情况下,邦克里酸的影响下线粒体内腺嘌呤核苷酸池的组成不变。(b) 被邦克里酸固定的添加的ADP和ATP可以被鉴定为AMP、ADP和ATP,其比例与内源性池中相同。(c) 结合的核苷酸对氧化磷酸化或解偶联剂刺激的去磷酸化的反应与内源性核苷酸相似。可以得出结论,在邦克里酸影响下固定于线粒体的ADP或ATP与线粒体内腺嘌呤核苷酸池平衡,并且在线粒体内磷酸盐转移反应中具有活性。结果与亲和力增加机制不一致,但支持重新定向机制,该机制假定在邦克里酸影响下,ADP和ATP以与添加邦克里酸之前外部可用载体位点数量相同的量被困在线粒体内。