The Reorganization Energy in Cytochrome c is Controlled by the Accessibility of the Heme to the Solvent

被引:50
作者
Bortolotti, Carlo Augusto [1 ]
Siwko, Magdalena E. [2 ,3 ]
Castellini, Elena [1 ]
Ranieri, Antonio [1 ]
Sola, Marco [1 ]
Corni, Stefano [3 ]
机构
[1] Univ Modena & Reggio Emilia, Dept Chem, I-41125 Modena, Italy
[2] Univ Modena & Reggio Emilia, Dept Phys, I-41125 Modena, Italy
[3] CNR, Inst Nanosci, Ctr S3, Modena, Italy
关键词
BIOLOGICAL ELECTRON-TRANSFER; 4-HELIX BUNDLE PROTEIN; TUNNELING PATHWAY; REDOX PROPERTIES; LINEAR-RESPONSE; DYNAMICS; FLUCTUATIONS; COMPLEXES; SPHERE; AZURIN;
D O I
10.1021/jz200734a
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Elucidation of the molecular determinants of the reorganization energy A is central to the understanding of fundamental biological processes based on energy transduction pathways. Here, we use a combined experimental/theoretical approach to electrochemically determine the reorganization energy for a number of cytochrome c variants and compute structure-related properties relevant to the kinetics of the electron transfer process through molecular dynamics simulations. We find that the exposure of the heme group to solvent controls the reorganization energy of the investigated proteins. Therefore, fine-tuning of the kinetics of the electron transfer process can be achieved through modulation of the accessibility of the iron to the surrounding water. Our findings lead the way for a new strategy for the design of protein-based bioelectronic materials, requiring fast and efficient electron transfer.
引用
收藏
页码:1761 / 1765
页数:5
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