BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS

FEIFAN LENG^1,*, WEN LUO¹, YANJUN JING¹, YUANLI LI1, QINGWEI WEI1, MINGJUN YANG1, YONGGANG WANG1,*, ABDOL GHAFFAR EBADI2

¹School of life science and engineering, Lanzhou University of Technology, Lanzhou 730050, China - ²Department of Agriculture, Jouybar branch, Islamic Azad University, Jouybar, Iran

Introduction: Ferredoxin was one of important proteins in Acidithiobacillus ferrooxidans, functioned as electron transfer agents in many important biological reactions. As a crucial protein involved in iron oxidation-reduction and electron transfer, tho- rough investigation of ferredoxin was of great significance. Aim of the study is to study the structure and function of ferredoxin laid a theoretical foundation for understanding energy accumulation, metabolism and electron transfer of Acidithiobacillus ferrooxidans.

Materials and methods: Eleven kinds of ferredoxin sequences were downloaded from the NCBI database. Aspects concluding basic physicochemical properties, conserved domain, protein modification, subcellular localization, advanced structures prediction, homology and protein interaction network were predicted on the application of combination of software and online tools.

Results: The results showed that all proteins were electrically neutral in acidic solution except ACK80487.1. Minority of the proteins (three to eleven) were hydrophilic protein. Majority of the proteins were unstable with exceptions of ACK79455.1 & ACK80389.1. The cytoplasm was the place where they played a part. Through the comprehensive forecast, four proteins were involved in nitrogen fixation reaction; two proteins mainly participated in iron sulfur-cluster assembly; four from eleven took effect in oxidation and reduction reactions; the rest one play a major role in nucleic acid reaction.

Conclusion: The basic physicochemical properties, the secondary structure and tertiary structure of protein, subcellular localization, signal peptide and transmembrane domain analysis showed the protein was characterized by diversity and implied the complexity of electron transfer and energy mechanism of Acidithiobacillus ferrooxidans