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Red phosphorus (RP) is an emerging visible‐light‐responsive photocatalyst, yet the rapid charge recombination has limited photocatalytic hydrogen production activity. In this work, a Z‐scheme heterostructure with RP nanolayer coated on high‐index (116) faceted anatase TiO2 nanoparticles (TiO2@RP) is designed and fabricated via chemical vapor deposition. Compared with pristine TiO2 and RP, the optimized TiO2@RP Z‐scheme heterostructure exhibits a significantly boosted photocatalytic activity for pure water splitting, with hydrogen evolution rate reaching 12.9 µmol·h−1, under simulated solar light irradiation. The strong interfacial interaction and staggered band alignment between (116) faceted TiO2 and RP result in the formation of built‐in electric field, which can drive the directional charge migration from the conduction band (CB) of TiO2 to the valance band (VB) of RP under light irradiation, with photoelectrons and holes of high redox ability maintained at the CB of RP and the VB of TiO2, respectively. This well‐designed heterostructure greatly promotes photogenerated charge separation and migration via a direct Z‐scheme charge transfer pathway. [ABSTRACT FROM AUTHOR]

In a calcium-dependent interaction critical for blood coagulation, vitamin K-dependent blood coagulation proteins bind cell membranes containing phosphatidylserine via ?-carboxyglutamic acid-rich (Gla) domains. Gla domain-mediated protein-membrane interaction is required for generation of thrombin, the terminal enzyme in the coagulation cascade, on a physiologic time scale. We determined by X-ray crystallography and NMR spectroscopy the lysophosphatidylserine-binding site in the bovine prothrombin Gla domain. The serine head group binds Gla domain-bound calcium ions and Gla residues 17 and 21, fixed elements of the Gla domain fold, predicting the structural basis for phosphatidylserine specificity among Gla domains. Gla domains provide a unique mechanism for protein-phospholipid membrane interaction. Increasingly Gla domains are being identified in proteins unrelated to blood coagulation. Thus, this membrane-binding mechanism may be important in other physiologic processes. [ABSTRACT FROM AUTHOR]