The corrosive anions (e.g., Cl⁻) have been recognized as the origins to cause severe corrosion of anode during seawater electrolysis, while in experiments it is found that natural seawater (~0.41 M Cl⁻) is usually more corrosive than simulated seawater (~0.5 M Cl⁻). Here we elucidate that besides Cl⁻, Br⁻ in seawater is even more harmful to Ni-based anodes because of the inferior corrosion resistance and faster corrosion kinetics in bromide than in chloride. Experimental and simulated results reveal that Cl⁻ corrodes locally to form narrow-deep pits while Br⁻ etches extensively to generate shallow-wide pits, which can be attributed to the fast diffusion kinetics of Cl⁻ and the lower reaction energy of Br⁻ in the passivation layer. Additionally, for the Ni-based electrodes with catalysts (e.g., NiFe-LDH) loading on the surface, Br⁻ causes extensive spalling of the catalyst layer, resulting in rapid performance degradation. This work clearly points out that, in addition to anti-Cl⁻ corrosion, designing anti-Br⁻ corrosion anodes is even more crucial for future application of seawater electrolysis.

The electrochemical synthesis of solid compounds is a critical emerging area in electrocatalysis; however, a major challenge is still remaining on severe catalysts scaling driven by strong solid-solid interactions, giving rise to rapid electrode deactivation. In this study, for the example of simultaneous synthesis of Mg(OH)₂ and H₂ from natural seawater electrolysis, we demonstrate that Pt catalyst with surface-coordinated halogens (F, Cl, Br, I) can alleviate this scaling effect (i.e., solidophobicity) by like-charge repulsion and thus regulating the local environment. Specifically, Pt-I coordination results in supersolidophobicity, achieving a successful extraction of Mg(OH)₂ ( > 99% purity) while stably producing H₂ (under 100 mA cm^-2 for over 5000 hours). A combination of experimental and theoretical studies reveals that, due to the like charge repulsion between I^- and in situ generated OH^-, the Pt-I catalyst regulates the surface pH gradient which increases the distance from the electrode surface to the Mg(OH)₂ nucleus (>4 μm) and facilitates homogeneous nucleation. Additionally, the scalability of the Pt-I catalyst, along with the techno-economic analysis and life cycle assessment of the natural seawater electrolysis technology are systematically demonstrated.

Bactericidal/permeability-increasing protein (BPI) is a 455-residue (∼55 kDa) protein found mainly in the primary (azurophilic) granules of human neutrophils. BPI is an endogenous antibiotic protein that belongs to the family of mammalian lipopolysaccharide (LPS)-binding and lipid transport proteins. Its major function is to kill Gram-negative bacteria, thereby protecting the host from infection. In addition, BPI can inhibit angiogenesis, suppress LPS-mediated platelet activation, increase DNA synthesis, and activate ERK/Akt signaling. In this study, we found that Bpi was expressed in the testis and epididymis but not in the seminal vesicles, prostate, and solidification glands. BPI expression in the epididymis increased upon upregulation of testosterone, caused by injection of GNRH. In orchidectomized mice, BPI expression was significantly reduced, but its expression was restored to 30% of control levels in orchidectomized mice that received supplementary testosterone. The number of sperm fused per egg significantly decreased after incubation with anti-BPI antiserum. These results suggest that BPI may take part in the process of sperm–oocyte fusion and play a unique and significant role in reproduction. Abstract Bactericidal/permeability-increasing protein (BPI) is a 455-residue (∼55 kDa) protein found mainly in the primary (azurophilic) granules of human neutrophils. BPI is an endogenous antibiotic protein that belongs to the family of mammalian lipopolysaccharide (LPS)-binding and lipid transport proteins. Its major function is to kill Gram-negative bacteria, thereby protecting the host from infection. In addition, BPI can inhibit angiogenesis, suppress LPS-mediated platelet activation, increase DNA synthesis, and activate ERK/Akt signaling. In this study, we found that Bpi was expressed in the testis and epididymis but not in the seminal vesicles, prostate, and solidification glands. BPI expression in the epididymis increased upon upregulation of testosterone, caused by injection of GNRH. In orchidectomized mice, BPI expression was significantly reduced, but its expression was restored to 30% of control levels in orchidectomized mice that received supplementary testosterone. The number of sperm fused per egg significantly decreased after incubation with anti-BPI antiserum. These results suggest that BPI may take part in the process of sperm–oocyte fusion and play a unique and significant role in reproduction.