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The oxygen evolution reaction is central to making chemicals and energy carriers using electrons. Combining the great tunability of enzymatic systems with known oxide-based catalysts can create breakthrough opportunities to achieve both high activity and stability. Here we report a series of metal hydroxide-organic frameworks (MHOFs) synthesized by transforming layered hydroxides into two-dimensional sheets crosslinked using aromatic carboxylate linkers. MHOFs act as a tunable catalytic platform for the oxygen evolution reaction, where the π-π interactions between adjacent stacked linkers dictate stability, while the nature of transition metals in the hydroxides modulates catalytic activity. Substituting Ni-based MHOFs with acidic cations or electron-withdrawing linkers enhances oxygen evolution reaction activity by over three orders of magnitude per metal site, with Fe substitution achieving a mass activity of 80 A [Formula: see text] at 0.3 V overpotential for 20 h. Density functional theory calculations correlate the enhanced oxygen evolution reaction activity with the MHOF-based modulation of Ni redox and the optimized binding of oxygenated intermediates., (© 2022. The Author(s), under exclusive licence to Springer Nature Limited.)

Hemoglobin and myoglobin are oxygen-binding proteins with S = 0 heme {FeO 2 } 8 active sites. The electronic structure of these sites has been the subject of much debate. This study utilizes Fe K-edge X-ray absorption spectroscopy (XAS) and 1s2p resonant inelastic X-ray scattering (RIXS) to study oxyhemoglobin and a related heme {FeO 2 } 8 model compound, [(pfp)Fe(1-MeIm)(O 2 )] (pfp = meso-tetra(α,α,α,α- o -pivalamido-phenyl)porphyrin, or TpivPP, 1-MeIm = 1-methylimidazole) (pfpO 2 ), which was previously analyzed using L-edge XAS. The K-edge XAS and RIXS data of pfpO 2 and oxyhemoglobin are compared with the data for low-spin Fe II and Fe III [Fe(tpp)(Im) 2 ] 0/+ (tpp = tetra-phenyl porphyrin) compounds, which serve as heme references. The X-ray data show that pfpO 2 is similar to Fe II , while oxyhemoglobin is qualitatively similar to Fe III , but with significant quantitative differences. Density-functional theory (DFT) calculations show that the difference between pfpO 2 and oxyhemoglobin is due to a distal histidine H bond to O 2 and the less hydrophobic environment in the protein, which lead to more backbonding into the O 2 A valence bond configuration interaction multiplet model is used to analyze the RIXS data and show that pfpO 2 is dominantly Fe II with 6-8% Fe III character, while oxyhemoglobin has a very mixed wave function that has 50-77% Fe III character and a partially polarized Fe-O 2 π-bond., Competing Interests: The authors declare no conflict of interest.

Inspired by the period-four oscillation in flash-induced oxygen evolution of photosystem II discovered by Joliot in 1969, Kok performed additional experiments and proposed a five-state kinetic model for photosynthetic oxygen evolution, known as Kok's S-state clock or cycle 1,2 . The model comprises four (meta)stable intermediates (S 0 , S 1 , S 2 and S 3 ) and one transient S 4 state, which precedes dioxygen formation occurring in a concerted reaction from two water-derived oxygens bound at an oxo-bridged tetra manganese calcium (Mn 4 CaO 5 ) cluster in the oxygen-evolving complex 3-7 . This reaction is coupled to the two-step reduction and protonation of the mobile plastoquinone Q B at the acceptor side of PSII. Here, using serial femtosecond X-ray crystallography and simultaneous X-ray emission spectroscopy with multi-flash visible laser excitation at room temperature, we visualize all (meta)stable states of Kok's cycle as high-resolution structures (2.04-2.08 Å). In addition, we report structures of two transient states at 150 and 400 µs, revealing notable structural changes including the binding of one additional 'water', Ox, during the S 2 →S 3 state transition. Our results suggest that one water ligand to calcium (W3) is directly involved in substrate delivery. The binding of the additional oxygen Ox in the S 3 state between Ca and Mn1 supports O-O bond formation mechanisms involving O5 as one substrate, where Ox is either the other substrate oxygen or is perfectly positioned to refill the O5 position during O 2 release. Thus, our results exclude peroxo-bond formation in the S 3 state, and the nucleophilic attack of W3 onto W2 is unlikely.

Multielectron catalytic reactions, such as water oxidation, nitrogen reduction, or hydrogen production in enzymes and inorganic catalysts often involve multimetallic clusters. In these systems, the reaction takes place between metals or metals and ligands to facilitate charge transfer, bond formation/breaking, substrate binding, and release of products. In this study, we present a method to detect X-ray emission signals from multiple elements simultaneously, which allows for the study of charge transfer and the sequential chemistry occurring between elements. Kβ X-ray emission spectroscopy (XES) probes charge and spin states of metals as well as their ligand environment. A wavelength-dispersive spectrometer based on the von Hamos geometry was used to disperse Kβ signals of multiple elements onto a position detector, enabling an XES spectrum to be measured in a single-shot mode. This overcomes the scanning needs of the scanning spectrometers, providing data free from temporal and normalization errors and therefore ideal to follow sequential chemistry at multiple sites. We have applied this method to study MnOx-based bifunctional electrocatalysts for the oxygen evolution reaction (OER) and the oxygen reduction reaction (ORR). In particular, we investigated the effects of adding a secondary element, Ni, to form MnNiOx and its impact on the chemical states and catalytic activity, by tracking the redox characteristics of each element upon sweeping the electrode potential. The detection scheme we describe here is general and can be applied to time-resolved studies of materials consisting of multiple elements, to follow the dynamics of catalytic and electron transfer reactions.

The protonation state of oxo bridges in nature is of profound importance for a variety of enzymes, including the Mn4CaO5 cluster of photosystem II and the Mn2O2 cluster in Mn catalase. A set of dinuclear bis-μ-oxo-bridged Mn(IV) complexes in different protonation states was studied by Kβ emission spectroscopy to form the foundation for unraveling the protonation states in the native complex. The valence-to-core regions (valence-to-core XES) of the spectra show significant changes in intensity and peak position upon protonation. DFT calculations were performed to simulate the valence-to-core XES spectra and to assign the spectral features to specific transitions. The Kβ(2,5) peaks arise primarily from the ligand 2p to Mn 1s transitions, with a characteristic low energy shoulder appearing upon oxo-bridge protonation. The satellite Kβ" peak provides a more direct signature of the protonation state change, since the transitions originating from the 2s orbitals of protonated and unprotonated μ-oxo bridges dominate this spectral region. The energies of the Kβ" features differ by ~3 eV and thus are well resolved in the experimental spectra. Additionally, our work explores the chemical resolution limits of the method, namely, whether a mixed (μ-O)(μ-OH2) motif can be distinguished from a symmetric (μ-OH)2 one. The results reported here highlight the sensitivity of Kβ valence-to-core XES to single protonation state changes of bridging ligands, and form the basis for further studies of oxo-bridged polymetallic complexes and metalloenzyme active sites. In a complementary paper, the results from X-ray absorption spectroscopy of the same Mn(IV) dimer series are discussed.

Advancing theories of how metal-oxygen bonding influences metal oxo properties can expose new avenues for innovation in materials science, catalysis, and biochemistry. Historically, spectroscopic analyses of the transition metal MO(4)(x-) anions have formed the basis for new M-O bonding theories. Herein, relative changes in M-O orbital mixing in MO(4)(2-) (M = Cr, Mo, W) and MO(4)(-) (M = Mn, Tc, Re) are evaluated for the first time by nonresonant inelastic X-ray scattering, X-ray absorption spectroscopy using fluorescence and transmission (via a scanning transmission X-ray microscope), and time-dependent density functional theory. The results suggest that moving from Group 6 to Group 7 or down the triads increases M-O e* (π*) mixing; for example, it more than doubles in ReO(4)(-) relative to CrO(4)(2-). Mixing in the t(2)* orbitals (σ* + π*) remains relatively constant within the same Group, but increases on moving from Group 6 to Group 7. These unexpected changes in orbital energy and composition for formally isoelectronic tetraoxometalates are evaluated in terms of periodic trends in d orbital energy and radial extension.