在第87位带有苯丙氨酸或酪氨酸的酵母细胞色素c将电子传递给（锌细胞色素c过氧化物酶）+的速率是第87位为丝氨酸或甘氨酸的变体的一万倍。
Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants.
作者信息
Liang N, Pielak G J, Mauk A G, Smith M, Hoffman B M
出版信息
Proc Natl Acad Sci U S A. 1987 Mar;84(5):1249-52. doi: 10.1073/pnas.84.5.1249.
Abstract
Of the many factors known to influence the rate of electron transfer between two metalloproteins, it is particularly difficult to assess the role of the polypeptide matrix intervening between the donor and acceptor sites. To determine whether the phylogenetically conserved Phe-87 of yeast iso-1-cytochrome c helps to mediate electron transfer between cytochrome c and cytochrome c peroxidase, we have constructed mutants of cytochrome c that are altered at this position and now have studied the kinetics of long-range electron transfer within their complexes with zinc-substituted cytochrome c peroxidase. We find that the rate of electron transfer from reduced cytochrome c to the zinc cytochrome c peroxidase pi-cation radical is four orders of magnitude greater when phenylalanine or tyrosine is present at position 87 than when serine or glycine is present.
摘要
在已知影响两种金属蛋白之间电子转移速率的众多因素中，特别难以评估介于供体和受体位点之间的多肽基质所起的作用。为了确定酵母同功酶-1-细胞色素c中系统发育保守的苯丙氨酸-87是否有助于介导细胞色素c与细胞色素c过氧化物酶之间的电子转移，我们构建了在该位置发生改变的细胞色素c突变体，并且现在已经研究了它们与锌取代的细胞色素c过氧化物酶形成的复合物内远程电子转移的动力学。我们发现，当87位存在苯丙氨酸或酪氨酸时，从还原型细胞色素c到锌细胞色素c过氧化物酶π-阳离子自由基的电子转移速率比存在丝氨酸或甘氨酸时快四个数量级。
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1
Yeast cytochrome c with phenylalanine or tyrosine at position 87 transfers electrons to (zinc cytochrome c peroxidase)+ at a rate ten thousand times that of the serine-87 or glycine-87 variants.在第87位带有苯丙氨酸或酪氨酸的酵母细胞色素c将电子传递给（锌细胞色素c过氧化物酶）+的速率是第87位为丝氨酸或甘氨酸的变体的一万倍。
Proc Natl Acad Sci U S A. 1987 Mar;84(5):1249-52. doi: 10.1073/pnas.84.5.1249.
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