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In this work, we report on the impedance of p-n junction-based Si biochips with gold ring top electrodes and unstructured platinum bottom electrodes which allows for counting target biomaterial in a liquid-filled ring top electrode region. The systematic experiments on p-n junction-based Si biochips fabricated by two different sets of implantation parameters (i.e. biochips PS5 and BS5) are studied, and the comparable significant change of impedance characteristics in the biochips in dependence on the number of bacteria suspension, i.e., Lysinibacillus sphaericus JG-A12, in Deionized water with an optical density at 600 nm from OD600 = 4–16 in the electrode ring region is demonstrated. Furthermore, with the help of the newly developed two-phase electrode structure, the modeled capacitance and resistance parameters of the electrical equivalent circuit describing the p-n junction-based biochips depend linearly on the number of bacteria in the ring top electrode region, which successfully proves the potential performance of p-n junction-based Si biochips in observing the bacterial suspension. The proposed p-n junction-based biochips reveal perspective applications in medicine and biology for diagnosis, monitoring, management, and treatment of diseases.

During the last years the interaction of U(VI) with the isolate Lysinibacillus sphaericus JG-A12, recovered from the uranium mining waste pile “Haberland” near Johanngeorgenstadt (JG), Saxony, Germany, was intensively studied [1, 2]. It could be demonstrated that L. sphaericus JG-A12 shows the ability to form S-layer proteins. This outermost subcellular structure plays an important role for selective binding of heavy metals, for example U(VI) [2]. The interaction of trivalent actinides (e.g., curium) with bacterial S-layer proteins is unknown. This knowledge is essential for the understanding of An(III) interactions at biological solid-water interfaces. Dependent on pH and [Ca] S-layer proteins occur as monomers and polymers in aqueous solution. The main aim of this study is to explore the unknown Cm(III) binding on different S-layers and S-layer protein structures. The direct speciation technique time-resolved laser-induced fluorescence spectroscopy (TRLFS) has been applied at trace Cm(III) concentrations. Two S-layer suspensions a) Ca-reduced protein containing 195 mmol Ca/mol protein and b) Ca-purified protein were investigated. As a result and illustrated in Figure 1, both S­layers have a high affinity to bind Cm(III) over a broad pH range between 3 and 9. The Ca-reduced S­layer proteins can associate Cm(III) in two coordination environments characterized by individual emission spectra and luminescence lifetimes (e.g., 140 and 300 µs). The results can be interpreted by an intensive Cm(III) interaction with S-layer monomers between pH 3 and 5 with monomer concentrations of 100, 60, and 17 %, respectively; and a dominating interaction with S-layer polymers between pH 6 to 9 with polymer concentrations of 84, 91, 91, and 75 %, respectively. Whereas in the Ca-purified S-layer protein suspension only one Cm(III) coordination environment occurs with a long lifetime of 300 µs. Here the S-layer monomers dominate the whole pH range. The Cm(III)-S-layer species with monom

During the last years the interaction of U(VI) with the isolate Lysinibacillus sphaericus JG-A12, recovered from the uranium mining waste pile “Haberland” near Johanngeorgenstadt (JG), Saxony, Germany, was intensively studied [1, 2]. It could be demonstrated that L. sphaericus JG-A12 shows the ability to form S-layer proteins. This outermost subcellular structure plays an important role for selective binding of heavy metals, for example U(VI) [2]. The interaction of trivalent actinides (e.g., curium) with bacterial S-layer proteins is unknown. This knowledge is essential for the understanding of An(III) interactions at biological solid-water interfaces. Dependent on pH and [Ca] S-layer proteins occur as monomers and polymers in aqueous solution. The main aim of this study is to explore the unknown Cm(III) binding on different S-layers and S-layer protein structures. The direct speciation technique time-resolved laser-induced fluorescence spectroscopy (TRLFS) has been applied at trace Cm(III) concentrations. Two S-layer suspensions a) Ca-reduced protein containing 195 mmol Ca/mol protein and b) Ca-purified protein were investigated. As a result and illustrated in Figure 1, both S­layers have a high affinity to bind Cm(III) over a broad pH range between 3 and 9. The Ca-reduced S­layer proteins can associate Cm(III) in two coordination environments characterized by individual emission spectra and luminescence lifetimes (e.g., 140 and 300 µs). The results can be interpreted by an intensive Cm(III) interaction with S-layer monomers between pH 3 and 5 with monomer concentrations of 100, 60, and 17 %, respectively; and a dominating interaction with S-layer polymers between pH 6 to 9 with polymer concentrations of 84, 91, 91, and 75 %, respectively. Whereas in the Ca-purified S-layer protein suspension only one Cm(III) coordination environment occurs with a long lifetime of 300 µs. Here the S-layer monomers dominate the whole pH range. The Cm(III)-S-layer species with monom

During the last years the interaction of U(VI) with the isolate Lysinibacillus sphaericus JG-A12, recovered from the uranium mining waste pile “Haberland” near Johanngeorgenstadt (JG), Saxony, Germany, was intensively studied [1, 2]. It could be demonstrated that L. sphaericus JG-A12 shows the ability to form S-layer proteins. This outermost subcellular structure plays an important role for selective binding of heavy metals, for example U(VI) [2]. The interaction of trivalent actinides (e.g., curium) with bacterial S-layer proteins is unknown. This knowledge is essential for the understanding of An(III) interactions at biological solid-water interfaces. Dependent on pH and [Ca] S-layer proteins occur as monomers and polymers in aqueous solution. The main aim of this study is to explore the unknown Cm(III) binding on different S-layers and S-layer protein structures. The direct speciation technique time-resolved laser-induced fluorescence spectroscopy (TRLFS) has been applied at trace Cm(III) concentrations. Two S-layer suspensions a) Ca-reduced protein containing 195 mmol Ca/mol protein and b) Ca-purified protein were investigated. As a result and illustrated in Figure 1, both S­layers have a high affinity to bind Cm(III) over a broad pH range between 3 and 9. The Ca-reduced S­layer proteins can associate Cm(III) in two coordination environments characterized by individual emission spectra and luminescence lifetimes (e.g., 140 and 300 µs). The results can be interpreted by an intensive Cm(III) interaction with S-layer monomers between pH 3 and 5 with monomer concentrations of 100, 60, and 17 %, respectively; and a dominating interaction with S-layer polymers between pH 6 to 9 with polymer concentrations of 84, 91, 91, and 75 %, respectively. Whereas in the Ca-purified S-layer protein suspension only one Cm(III) coordination environment occurs with a long lifetime of 300 µs. Here the S-layer monomers dominate the whole pH range. The Cm(III)-S-layer species with monom