Fragata M, Bellemare F
Biophys Chem. 1983 Oct;18(3):207-10. doi: 10.1016/0301-4622(83)80033-7.
Koppenol's rejection (Biophys. Chem. 18 (1983) 203) of a model of polarity-dependent ferrocytochrome c oxidation (M. Fragata and F. Bellemare, Biophys. Chem. 15 (1982) 111) places emphasis on the role of the protein surface charges in reactivity but is at the same time too restrictive as it neglects largely the polarity (dielectric constant) of the aqueous and hydrophobic interfaces of the exposed heme edge and the inner cleft (heme crevice) of cytochrome c which appear to be the oxidation-reduction sites. It is suggested that a more general model should take into account (i) a recognition (or diffusion) step where the distance travelled by cytochrome c at the membrane surface and/or the Brownian displacements in the bulk solution are greatly influenced by ionic strength, and (ii) a redox step where low polarity effects prevail with concomitant weakening of ionic activity.
科彭诺尔对极性依赖性亚铁细胞色素c氧化模型（M. 弗拉加塔和F. 贝勒马尔，《生物物理化学》15 (1982) 111）的否定（《生物物理化学》18 (1983) 203）强调了蛋白质表面电荷在反应性中的作用，但同时又过于局限，因为它在很大程度上忽略了暴露的血红素边缘的水相和疏水界面以及细胞色素c内部裂隙（血红素裂隙）的极性（介电常数），而这些似乎是氧化还原位点。有人提出，一个更通用的模型应考虑：(i) 一个识别（或扩散）步骤，其中细胞色素c在膜表面移动的距离和/或在本体溶液中的布朗位移受离子强度的极大影响；以及 (ii) 一个氧化还原步骤，其中低极性效应占主导，同时离子活性减弱。
