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Int J Mol Sci. 2013 Jun 19;14(6):12843-52. doi: 10.3390/ijms140612843.

Reconstructing a flavodoxin oxidoreductase with early amino acids.

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  • 1School of Life Sciences, Shandong Normal University, Jinan 250014, China. lumingfeng4659@sina.com.cn.

Abstract

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 Em,7 (fld) reached -360 mV, indicating that the flavodoxin mutant constituted solely by early amino acids can exert effective electron transfer activity.

PMID:
23783279
[PubMed - indexed for MEDLINE]
PMCID:
PMC3709815
Free PMC Article
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