Crowley Peter B, Ubbink Marcellus
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Acc Chem Res. 2003 Oct;36(10):723-30. doi: 10.1021/ar0200955.
Plastocyanin and cytochrome c(6) function as electron shuttles between cytochrome f and photosystem I in the photosynthetic redox chain. To transfer electrons the partners form transient complexes, which are remarkably short-lived (milliseconds or less). Recent nuclear magnetic resonance studies have revealed details of the molecular interfaces found in such complexes. General features include a small binding site with a hydrophobic core and a polar periphery, including some charged residues. Furthermore, it was found that the interactions are relatively nonspecific. The structural information, in combination with kinetic and theoretical analyses of protein complexes, provides new insight into the nature of transient protein interactions.
质体蓝素和细胞色素c(6)在光合氧化还原链中作为细胞色素f和光系统I之间的电子穿梭体发挥作用。为了传递电子，这些伙伴形成短暂的复合物，其寿命非常短（毫秒或更短）。最近的核磁共振研究揭示了此类复合物中分子界面的细节。一般特征包括一个具有疏水核心和极性外围的小结合位点，其中包括一些带电荷的残基。此外，还发现这些相互作用相对非特异性。该结构信息与蛋白质复合物的动力学和理论分析相结合，为瞬态蛋白质相互作用的本质提供了新的见解。
