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王勰博士学术报告
发布时间:2019-11-15 09:38:33     文章来源:www.402.com 发布者:汪的华     浏览次数:

报告题目:Presentation title: Biochemical and electrochemical studies of metalloproteins involved in oxygen reduction pathway in Acidithiobacillus ferrooxidans

报告人:王勰  博士 CNRS IMM CapEnergies BIP (Bioénergétique et Ingénierie des Protéines) - Marseille

报告时间:2019年11月15日(星期五)下午4点

报告地点:学院301会议室

Abstract:

Acidithiobacillus ferrooxidans is one of the most studied bacterial models to understand how to survive in an acid environment. Although several metalloproteins have been identified and characterized from a biochemical point of view, the electron transfer pathway (ET) of the respiratory chain coupling the oxidation of ferrous iron with the reduction of oxygen in this organism has not been elucidated. In our work, after having optimized the growth conditions of the bacterium and the production of the redox proteins involved, we reconstituted on the electrochemical interface part of the respiratory chain of A. ferrooxidans for the purpose of determining step by step the ET. Our attention focused on three proteins that interact in the respiratory chain: cytochrome c oxidase (CcO), the cupredoxin AcoP, which co-purifies with CcO but of unknown function, and a cytochrome dihemic (Cyt c4) proposed as interacting with the CcO. The demonstration, then the quantification of an intermolecular ET between the Cyt c4 and AcoP, then between the Cyt c4 and the CcO allowed us to propose a role for AcoP and a new pathway for the ET to the CcO. We then studied the electrochemical properties of CcO with respect to the catalytic reduction of O2. We have demonstrated the strong affinity of this oxidase for O2. We have established the chemical functions required to obtain a direct wiring of the enzyme on carbon nanomaterials. This showed that A. ferrooxidans CcO reduced O2 at potentials 500 mV more anodic than neutrophilic CcOs. Affinity for O2 and high redox potential make this CcO an enzyme of choice to develop a new generation of enzymatic fuel cells.




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