Orbital‐Selective Modulation of Spatial <i> p <sub>z</sub> ‐s </i> Hybridization for Enhanced Photocatalytic H <sub>2</sub> Evolution: Insights From NiSe@ReS <sub>2+</sub> <i> <sub>x</sub> </i> Cocatalyst
Regulating the p orbital structure of nonmetal active sites is a potential strategy to optimize hydrogen adsorption. However, existing modification ideas primarily focus on the total energy of the p orbitals, while overlooking the crucial spatial information of the multiple projected p<sub>x</sub>, p<sub>y</sub>, and p<sub>z</sub> orbitals, causing a random and nondirectional orbital modification. Herein, we propose a spatial orbital-selective modulation engineering to realize precise and efficient optimization of H adsorption on a core-shell NiSe@ReS<sub>2+</sub> <sub>x</sub> cocatalyst. Theoretical calculations find that the H adsorption intrinsically originates from the selective hybridization between individual S p<sub>z</sub> and H 1s orbitals (p<sub>z</sub>-s), which unlocks a most direct approach to optimize H adsorption. Based on this, we demonstrate that H adsorption on S sites is directionally weakened by selectively charging spatial S p<sub>z</sub> from NiSe to produce electron-rich p<sub>z</sub> <sup>δ-</sup> orbitals. This process increases the projected antibonding-orbital occupancy, weakens the spatial p<sub>z</sub>-s hybridization, and lowers the H<sub>2</sub>-formation energy barrier of ReS<sub>2+</sub> <sub>x</sub>, ultimately achieving an improved H<sub>2</sub>-evolution activity. This work offers spatial orbital-level insights into precisely designing effective catalysts for artificial photosynthesis.
Authors
- Duoduo Gao (ORCID: https://orcid.org/0009-0000-4762-5663)
- Huan Yu (ORCID: https://orcid.org/0000-0001-6078-8192)
- Chuanjia Jiang
- Hermenegildo Garcia
- Jianjun Zhang
- Jiaguo Yu
Institutions
- Nankai University (CN)
- China University of Geosciences (CN)
- Instituto de Tecnología Química (ES)
- Universitat Politècnica de València (ES)
Publication Details
- Journal
- Angewandte Chemie International Edition
- Published
- 2026-03-27
- DOI
- https://doi.org/10.1002/anie.2317803
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00