Alternative ground states enable pathway switching in biological electron transfer

被引:30
作者
Abriata, Luciano A. [1 ]
Alvarez-Paggi, Damian [2 ,3 ]
Ledesma, Gabriela N. [4 ]
Blackburn, Ninian J. [5 ]
Vila, Alejandro J. [1 ]
Murgida, Daniel H. [2 ,3 ]
机构
[1] Univ Nacl Rosario, Inst Biol Mol & Celular Rosario, Consejo Nacl Invest Cient & Tecn, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Santa Fe, Argentina
[2] Univ Buenos Aires, Dept Quim Inorgan Anal & Quim Fis, Buenos Aires, DF, Argentina
[3] Univ Buenos Aires, Fac Ciencias Exactas & Nat, Inst Quim Fis Mat Medio Ambiente & Energia INQUIM, Consejo Nacl Invest Cient & Tecn, Buenos Aires, DF, Argentina
[4] Univ Nacl Rosario, Inst Quim Rosario, Consejo Nacl Invest Cient & Tecn, Fac Ciencias Bioquim & Farmaceut, RA-2000 Rosario, Santa Fe, Argentina
[5] Oregon Hlth & Sci Univ, Inst Environm Hlth, Beaverton, OR 97006 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
cytochrome oxidase; invisible states; paramagnetic proteins; NMR; spectroscopy; CYTOCHROME-C-OXIDASE; TRANSFER COMPLEX; A SITE; REORGANIZATION ENERGY; SOLUBLE DOMAIN; TRANSFER RATES; BA(3) OXIDASE; PROTEIN; NMR; SPECTROSCOPY;
D O I
10.1073/pnas.1204251109
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Electron transfer is the simplest chemical reaction and constitutes the basis of a large variety of biological processes, such as photosynthesis and cellular respiration. Nature has evolved specific proteins and cofactors for these functions. The mechanisms optimizing biological electron transfer have been matter of intense debate, such as the role of the protein milieu between donor and acceptor sites. Here we propose a mechanism regulating long-range electron transfer in proteins. Specifically, we report a spectroscopic, electrochemical, and theoretical study on WT and single-mutant Cu-A redox centers from Thermus thermophilus, which shows that thermal fluctuations may populate two alternative ground-state electronic wave functions optimized for electron entry and exit, respectively, through two different and nearly perpendicular pathways. These findings suggest a unique role for alternative or "invisible" electronic ground states in directional electron transfer. Moreover, it is shown that this energy gap and, therefore, the equilibrium between ground states can be fine-tuned by minor perturbations, suggesting alternative ways through which protein-protein interactions and membrane potential may optimize and regulate electron-proton energy transduction.
引用
收藏
页码:17348 / 17353
页数:6
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