ArticleExtremophiles : life under extreme conditions2006
Structural analysis of the HiPIP from the acidophilic bacteria: Acidithiobacillus ferrooxidans.
Article in Extremophiles : life under extreme conditions, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 15 citations in OpenAlex.
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- A Model of Aerobic and Anaerobic Metabolism of Hydrogen in the ExtremophileFrontiers in microbiology · 2020Article
- Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications.Extremophiles : life under extreme conditions · 2012Review
- Structure at 1.0 A resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
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6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hip is a high-potential iron-sulfur protein (HiPIP) isolated from the acidophilic bacterium, Acidithiobacillus ferrooxidans. In the present work, a structural model of Hip suggests that the role of proline residues is essential to stabilize the protein folding at very low pH. The presence of an unusual disulfide bridge in Hip is demonstrated using mass spectrometry and nuclear magnetic resonance. This disulfide bridge is necessary to anchor the N-terminal extremity of the protein, but is not involved in the acid stability of Hip. The structural parameters correlated with the pH dependence of Hip redox potential are also analysed on the basis of this model. Given that the same structural features can enhance acidic stability and lead to elevated redox potentials, modulation of the redox potentials of electron carriers may be necessary to achieve electron transfer at very low pH.
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