BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS

doi:10.19193/0393-6384_2017_6_172

	BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS
	Leng, Feifan 2; Luo, Wen 2; Jing, Yanjun 2; Li, Yuanli 2; Wei, Qingwei 2; Yang, Mingjun 2; Wang, Yonggang 2; Ebadi, Abdol Ghaffar 1
刊名	ACTA MEDICA MEDITERRANEA
	2017
卷号	33 期号:6 页码:1085-1091
关键词	Acidithiobacillus ferrooxidans Bioinformatics analysis Electron transfer Interaction network Tertiary structure
ISSN号	0393-6384
DOI	10.19193/0393-6384_2017_6_172
英文摘要	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, thorough 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
WOS研究方向	General & Internal Medicine
语种	英语
出版者	CARBONE EDITORE
WOS记录号	WOS:000411949500031
内容类型	期刊论文
源URL	[http://ir.lut.edu.cn/handle/2XXMBERH/155439]
专题	生命科学与工程学院
作者单位	1.Islamic Azad Univ, Jouybar Branch, Dept Agr, Jouybar, Iran 2.Lanzhou Univ Technol, Sch Life Sci & Engn, Lanzhou 730050, Gansu, Peoples R China;
推荐引用方式 GB/T 7714	Leng, Feifan,Luo, Wen,Jing, Yanjun,et al. BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS[J]. ACTA MEDICA MEDITERRANEA,2017,33(6):1085-1091.
APA	Leng, Feifan.,Luo, Wen.,Jing, Yanjun.,Li, Yuanli.,Wei, Qingwei.,...&Ebadi, Abdol Ghaffar.(2017).BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS.ACTA MEDICA MEDITERRANEA,33(6),1085-1091.
MLA	Leng, Feifan,et al."BIOINFORMATICS ANALYSIS OF FERREDOXIN FROM ACIDITHIOBACILLUS FERROOXIDANS".ACTA MEDICA MEDITERRANEA 33.6(2017):1085-1091.