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首页> 外文期刊>Applied Microbiology >New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph
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New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph

机译：专一的铁氧化化合自养生物的蛋白质组学特征揭示了对微生物铁氧化的新见解。

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Microaerophilic, neutrophilic, iron-oxidizing bacteria (FeOB) grow via the oxidation of reduced Fe(II) at or near neutral pH, in the presence of oxygen, making them relevant in numerous environments with elevated Fe(II) concentrations. However, the biochemical mechanisms for Fe(II) oxidation by these neutrophilic FeOB are unknown, and genetic markers for this process are unavailable. In the ocean, microaerophilic microorganisms in the genus Mariprofundus of the class Zetaproteobacteria are the only organisms known to chemolithoautotrophically oxidize Fe and concurrently biomineralize it in the form of twisted stalks of iron oxyhydroxides. The aim of this study was to identify highly expressed proteins associated with the electron transport chain of microaerophilic, neutrophilic FeOB. To this end, Mariprofundus ferrooxydans PV-1 was cultivated, and its proteins were extracted, assayed for redox activity, and analyzed via liquid chromatography-tandem mass spectrometry for identification of peptides. The results indicate that a cytochrome c _(4), cbb _(3)-type cytochrome oxidase subunits, and an outer membrane cytochrome c were among the most highly expressed proteins and suggest an involvement in the process of aerobic, neutrophilic bacterial Fe oxidation. Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus .
机译：需氧的中性嗜中性铁氧化细菌（FeOB）在氧气存在下通过还原的Fe（II）在中性pH或接近中性pH的条件下氧化而生长，从而使它们在Fe（II）浓度升高的许多环境中都具有重要意义。但是，这些嗜中性FeOB氧化Fe（II）的生化机制尚不清楚，并且该过程的遗传标记也不可用。在海洋中，Zetaproteobacteria类的Mariprofundus属中的微需氧微生物是唯一已知的化学自养生性氧化Fe并同时以扭曲的羟基氧化铁茎形式生物矿化的生物。这项研究的目的是鉴定与嗜微嗜中性FeOB的电子转运链相关的高表达蛋白质。为此，培养了Mariprofundus ferrooxydans PV-1，提取其蛋白质，测定其氧化还原活性，并通过液相色谱-串联质谱法进行分析以鉴定肽。结果表明，细胞色素c _（4），cbb _（3）型细胞色素氧化酶亚基和外膜细胞色素c是表达最强的蛋白质，并提示其参与有氧嗜中性细菌Fe氧化过程。与替代复合物III，磷酸盐转运，碳固定和生物膜形成相关的蛋白质丰富，与Mariprofundus的生活方式一致。

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