Reconstructing a Flavodoxin Oxidoreductase with Early Amino Acids

International Journal of Molecular Sciences

Ming-Feng Lu³  Hong-Fang Ji¹  Ting-Xuan Li²  Shou-Kai Kang²  Yue-Jie Zhang¹  Jue-Fei Zheng²  Tian Tian²  Xi-Shuai Jia²  Xing-Ming Lin² 

[1] School of Life Sciences, Shandong University of Technology, Zibo 255091, China; E-Mails:;National Key Laboratory of Crop Genetic Improvement, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China; E-Mails:;School of Life Sciences, Shandong Normal University, Jinan 250014, China

关键词: origin of life;    primitive redox protein;    cofactor;    early amino acid;   

DOI  :  10.3390/ijms140612843

来源: mdpi

【 摘 要 】

Primitive proteins are proposed to have utilized organic cofactors more frequently than transition metals in redox reactions. Thus, an experimental validation on whether a protein constituted solely by early amino acids and an organic cofactor can perform electron transfer activity is an urgent challenge. In this paper, by substituting “late amino acids (C, F, M, T, W, and Y)” with “early amino acids (A, L, and V)” in a flavodoxin, we constructed a flavodoxin mutant and evaluated its characteristic properties. The major results showed that: (1) The flavodoxin mutant has structural characteristics similar to wild-type protein; (2) Although the semiquinone and hydroquinone flavodoxin mutants possess lower stability than the corresponding form of wild-type flavodoxin, the redox potential of double electron reduction E_m,7 (fld) reached −360 mV, indicating that the flavodoxin mutant constituted solely by early amino acids can exert effective electron transfer activity.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland