Functional Roles of the Aromatic Residues in the Stabilization of the [$Fe_4S_4$] Cluster in the Iro Protein from Acidithiobacillus ferrooxidans

Functional Roles of the Aromatic Residues in the Stabilization of the [$Fe_4S_4$] Cluster in the Iro Protein from Acidithiobacillus ferrooxidans
Functional Roles of the Aromatic Residues in the Stabilization of the [$Fe_4S_4$] Cluster in the Iro Protein from Acidithiobacillus ferrooxidans

ㆍ 저자명: Zeng. Jia,Liu. Qing,Zhang. Xiaojian,Mo. Hongyu,Wang. Yiping,Chen. Qian,Liu. Yuandong
ㆍ 간행물명: Journal of microbiology and biotechnology
ㆍ 권/호정보: 2010년|20권 2호|pp.294-300 (7 pages)
ㆍ 발행정보: 한국미생물생명공학회
ㆍ 파일정보: 정기간행물|ENG|
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ㆍ 주제분야: 기타

이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.

서지반출

기타언어초록

The Iro protein is a member of the HiPIP family with the [$Fe_4S_4$] cluster for electron transfer. Many reports proposed that the conserved aromatic residues might be responsible for the stability of the iron-sulfur cluster in HiPIP. In this study, Tyr10 was found to be a critical residue for the stability of the [$Fe_4S_4$] cluster, according to site-directed mutagenesis results. Tyr10, Phe26, and Phe48 were essential for the stability of the [$Fe_4S_4$] cluster under acidic condition. Trp44 was not involved in the stability of the [$Fe_4S_4$] cluster. Molecular structure modeling for the mutant Tyr10 proteins revealed that the aromatic group of Tyr10 may form a hydrophobic barrier to protect the [$Fe_4S_4$] cluster from solvent.

키워드

Acidithiobacillus ferrooxidans Iro protein iron-sulfur cluster mutation molecular modeling

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