Probing heavy metal binding to phycobiliproteins.
Probing heavy metal binding to phycobiliproteins.
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探测重金属结合与植物脂蛋白的结合。
DOI:
10.1111/febs.16396
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发表时间:
2022-08
期刊:
影响因子:
--
通讯作者:
中科院分区:
文献类型:
--
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Blue‐green algae, also known as cyanobacteria, contain some of the most efficient light‐harvesting complexes known. These large, colourful complexes consist of phycobiliproteins which are extremely valuable in the cosmetics, food, nutraceutical and pharmaceutical industries. Additionally, the colourful and fluorescent properties of phycobiliproteins can be modulated by metal ions, making them highly attractive as heavy metal sensors and heavy metal scavengers. Although the overall quenching ability metal ions have on phycobiliproteins is known, the mechanism of heavy metal binding to phycobiliproteins is not fully understood, limiting their widespread quantitative applications. Here, we show using high‐resolution native mass spectrometry that phycobiliprotein complexes bind metal ions in different manners. Through monitoring the binding equilibria and metal‐binding stoichiometry, we show in particular copper and silver to have drastic, yet different effects on phycobiliprotein structure, both copper and silver modulate the overall complex properties. Together, the data reveals the mechanisms by which metal ions can modulate phycobiliprotein properties which can be used as a basis for the future design of metal‐related phycobiliprotein applications. Native mass spectrometry reveals differential binding of metal ions to the colourful fluorescent phycobiliproteins from cyanobacteria. The results presented in this study have a broad impact on the use of phycobiliproteins in biosensors and in predicting the response of cyanobacteria to heavy‐metal contaminants within the environment.
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