Bacterial protein could help find materials for your next smartphone

Bacterial protein could help find materials for your next smartphone

A structural model of the compact metal-bound form of the lanmodulin protein, which is 100-million times better at binding to lanthanides--the rare-earth metals used in smartphones and other technologies--than to other metals like calcium.

Credit: Penn State

A newly discovered protein can help detect, target and collect rare-earth metals used in smartphones. Protein is described in two new studies done by researchers from Penn State, which is 100 million times better when binding to lanthanides - Rare-Earth metals used in smartphones and other technologies - Comparison of other metals like calcium In. The first study, which appears in the American Chemical Society's journal, describes the protein, and the second paper, which appears online in journal biochemistry, describes its unique structure, which is potentially notable for the lanthanides Plays a role in selection.

"Recently, there is a lot of interest in expanding access to rare-earth elements such as lanthanides , which are used in smartphones, hybrid car batteries, lasers and other technologies," said Joseph Cotruvo Jr., in Penn State chemistry Assistant Professor and Louis Martarano  Career Development Professor and author of both studies. "Because the physical properties of rare-earth elements are alike, it can be difficult to target and collect, especially to anyone. Understanding how this protein binds lanthanides with such incredibly high selectivity, these important metals Can reveal ways to detect and target. "

The research team discovered proteins, which they named lanmodulin, inside the bacterial methylobacterium, which grows on the leaves and soil of plants and plays an important role in how carbon moves through the environment. Bacteria require lanthanides for the proper functioning of some of their enzymes, in which a bacteria helps to process carbon, which is essential for its development.

Cotruvo said, "These bacteria require other metals such as lanthanides and calcium to grow." "They need a way to get each metal out of the environment and should ensure that they go to the right place within each cell. It appears that these bacteria develop a unique way to target the lanthanides in the environment. , Where they are very abundant. Other metals such as calcium. "

The unique structure of proteins, which Cotruvo determined in collaboration with the laboratory of Chemistry Associate Professor Scott Shelter, can explain why it is 100 million times better to build lanthanides on calcium. In the absence of metals,  Cotruvo explained that the protein is mostly unstructured, but when the metal is present, it transforms the composition into a compact, well-defined structure.

The new compact form consists of four structures called "EF hand". Human cells have many proteins with EF hands, which are involved in using calcium for functions such as neurons firing and contraction of the muscles. These proteins also form lanthanides, although lanthanides are not physically relevant in humans, and protein is only 10 or 100 times more likely than lactaneids to bind calcium. The compact structure of laminodulin protein also contains amino acids, which is called proline in each of the EF hands in a unique position, which can contribute to the lanthanides selectivity of the protein.

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Cotruvo said, "The mechanism of selectivity of lanmondide for lanthanides  is not yet clear, but we feel that it comes down to the structural changes occurring in the presence of metal," Cotruvo  said. "This structural change is important for the functioning of the protein; For example, some protein-protein interactions can occur only when the protein is in its compact form. To inspire a transformational change, a very small quantity of lanthanides is needed. , But it will take too much. More calcium, more than bacteria, can actually lead to change. Together, it will help to ensure selectivity for lanthanides . "

To understand how protein is selective, mining for industrial purposes can provide insights into the collection of lanthanides with extraction from the waste streams.

Cotruvo said, "Processing these currents to separate rare metals from the earth is challenging in a challenging way," both said, "due to the abundance of rare earth and their impurity, they need to keep acid in large amounts. it occurs." Solution. Reducing pH usually reduces intimacy towards metals, but we feel that this protein starts with such high affinity, which can help to overcome these challenges. We are currently investigating this possibility. "

Apart from searching for the selectivity of proteins and the work of amino acids located specifically, the research team is also detecting the protein intake for other metals, because lanthanides  is often found in the presence of iron, manganese and other metals, And aluminum, which are in greater abundance.

"We are also very interested in the biological work of proteins," said Cotruvo . "But ultimately we hope that understanding the protein will create more environmentally friendly ways to achieve rare-earth metals from the environment."