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Oxygen-evolving complex

The oxygen-evolving complex (OEC), also known as the water-splitting or water-oxidizing complex, is an inorganic cofactor embedded within the lumenal side of photosystem II (PSII), a multi-subunit protein-pigment complex located in the thylakoid membranes of chloroplasts in plants, algae, and cyanobacteria.^[1] It catalyzes the light-driven oxidation of two water molecules to produce one molecule of dioxygen (O₂), four protons (H⁺), and four electrons (e⁻), a four-electron process that couples to the one-electron photochemistry of PSII to drive the oxygenic photosynthesis essential for life on Earth.^[2]^[1] The OEC's catalytic core is an oxo-bridged Mn₄CaO₅ cluster arranged in a distorted chair-like topology, where four manganese (Mn) ions and one calcium (Ca) ion are bridged by five oxygen atoms and coordinated by carboxylate and histidine residues from the D1 and CP43 subunits of PSII.^[2]^[1] This cluster undergoes a catalytic cycle known as the S-state cycle or Kok cycle, progressing through five redox states (S₀ to S₄), with each transition triggered by light-induced charge separation at the PSII reaction center (P680) and involving sequential oxidation of the Mn ions, proton release, and eventual O–O bond formation and O₂ evolution during the S₃ → (S₄) → S₀ step.^[2]^[1] Structural studies, including time-resolved serial femtosecond crystallography, have revealed dynamic changes in Mn–Mn and Mn–ligand distances (typically ~2.7–2.8 Å) across S-states, along with water insertion via channels like O1 and O4, and the role of chloride ions in facilitating proton egress.^[2]^[1] Beyond its fundamental role in generating atmospheric oxygen and sustaining the global biosphere, the OEC has inspired biomimetic research for artificial photosynthesis and sustainable energy production, given its efficiency in multi-electron water oxidation under mild conditions.^[2] Ongoing advances in high-resolution cryo-electron microscopy and X-ray spectroscopy continue to refine models of its mechanism, including proton-coupled electron transfer and substrate water binding sites.^[2]^[1]

Overview

Definition and Biological Role

The oxygen-evolving complex (OEC) is a Mn₄CaO₅ cluster that functions as the catalytic site for the four-electron oxidation of two water molecules during oxygenic photosynthesis.^[3]^[4] This cluster, embedded within photosystem II, enables the extraction of electrons from water to replenish those lost during light-driven charge separation.^[5] The overall reaction catalyzed by the OEC is:

$2 \mathrm{H_2O} \rightarrow \mathrm{O_2} + 4 \mathrm{H^+} + 4 \mathrm{e^-}

This process requires a thermodynamic potential of 1.23 V versus the normal hydrogen electrode at standard conditions (pH 0), though in the physiological context of pH ~7, the effective potential is approximately 0.82 V.^[6] Biologically, the OEC supplies electrons to the photosynthetic electron transport chain, driving the reduction of NADP⁺ to NADPH and contributing to proton gradients for ATP synthesis.^[5] Simultaneously, it generates molecular oxygen as a byproduct, which accumulates in the atmosphere and supports aerobic respiration across diverse organisms.^[7] The evolutionary emergence of the OEC in cyanobacteria around 2.4 billion years ago represented a transformative innovation in biology, initiating the Great Oxidation Event that irreversibly oxygenated Earth's atmosphere and oceans.^[8]^[9] This event not only enabled the proliferation of oxygen-dependent life but also profoundly altered global geochemistry by facilitating the deposition of banded iron formations and shifting the redox state of the planet.^[8]

Integration with Photosystem II

The oxygen-evolving complex (OEC) is positioned on the lumenal side of the thylakoid membrane in photosystem II (PSII), where it is embedded and bound primarily to the D1 and CP43 core subunits of the complex. This strategic location positions the OEC to facilitate water oxidation in the thylakoid lumen, enabling the release of protons and oxygen into the intra-thylakoid space. The binding involves direct coordination with polypeptide loops from D1 and CP43, ensuring the OEC's proximity to the reaction center for efficient electron transfer.^[10]^[1] The OEC engages in extensive interactions with surrounding amino acid residues that provide ligands and stabilize its structure. Key ligands include aspartates such as D1-Asp170 and D1-Asp342, glutamates like D1-Glu189, D1-Glu333, and CP43-Glu354, and histidines such as D1-His332 from the D1 subunit, along with arginine residues like CP43-Arg357. These residues form carboxylate bridges and hydrogen bonds that anchor the inorganic cluster. Extrinsic proteins PsbO, PsbV, and PsbU further enhance this integration by binding to the lumenal surface, interacting with D1 and CP43 loops through hydrogen bonding networks involving aspartates, glutamates, and histidines, thereby shielding the OEC and optimizing its catalytic environment in cyanobacteria and similar organisms.^[10]^[11] Within PSII, the OEC plays a central role in charge separation by serving as the ultimate electron donor. Upon photoexcitation of the primary donor P680, electrons are rapidly transferred through the reaction center, oxidizing the tyrosine residue Yz (D1-Tyr161), which is hydrogen-bonded near the OEC; the OEC then replenishes the electron by advancing through its S-state cycle during water oxidation. This integration ensures sustained electron flow from water to the PSII acceptor side, preventing oxidative damage to the reaction center.^[10] The structural integrity of the OEC-PSII assembly relies on Ca²⁺ and Cl⁻ ions, with Ca²⁺ forming a core part of the Mn₄CaO₅ cluster to bridge manganese ions and maintain the cubane-like geometry, while Cl⁻ ions bind at specific sites near the cluster to modulate ligand conformations and proton release pathways. These ions contribute to overall stability by preventing disassembly under physiological conditions. Mutations in OEC binding sites, such as replacement of D1-Asp170 or CP43-Arg357, disrupt these interactions, leading to impaired PSII assembly, reduced Mn cluster formation, and diminished oxygen evolution activity, as observed in site-directed mutagenesis studies in cyanobacteria.^[10]^[11]^[12]

Structural Features

Chemical Composition

The oxygen-evolving complex (OEC) features a core Mn₄CaO₅ cluster consisting of four manganese ions (Mn), one calcium ion (Ca), and five oxygen atoms that function as μ-oxo bridges linking the metal centers. This cubane-like arrangement forms the catalytic site for water oxidation in photosystem II.^[10] In the dark-adapted S₁ state, the manganese ions adopt oxidation states of two Mn(III) and two Mn(IV), providing the necessary redox potential for sequential electron abstraction during the catalytic cycle. Additionally, four water-derived ligands—typically two hydroxide or aqua groups on Mn₄ and two on Ca—coordinate the cluster, potentially serving as substrates or proton relays in the reaction.^[10] The OEC's function is supported by inorganic cofactors, including chloride (Cl^-) and bicarbonate (HCO₃^-) ions. Two chloride ions are positioned adjacent to the cluster, enhancing Mn²⁺ oxidation during assembly and inhibiting non-productive hydrogen peroxide formation to ensure efficient dioxygen evolution. Bicarbonate acts as an essential cofactor in the photoactivation process, facilitating the reconstitution of the Mn₄CaO₅ core and stabilizing its activity under physiological conditions.^[13]^[2]^[14]

Three-Dimensional Arrangement

The three-dimensional arrangement of the oxygen-evolving complex (OEC) is characterized by a Mn₄CaO₅ cluster in a distorted chair topology. This structure features a cubane-like Mn₃CaO₄ core composed of three manganese ions (Mn1–Mn3) and one calcium ion, bridged by μ-oxo ligands O1, O2, O3, and O5, with the fourth manganese ion (Mn4) serving as a dangling component attached to the core via oxo bridges O4 (to Mn3) and O5 (shared).^[15] This open cubane configuration positions the metals in a manner that facilitates substrate access and electron transfer during catalysis. X-ray crystallographic studies at resolutions around 1.9 Å have elucidated key geometric parameters, including Mn–Mn distances typically spanning 2.7–3.3 Å—such as shorter di-μ-oxo-bridged interactions near 2.7 Å and a longer distance of approximately 3.3 Å between Mn4 and the cubane—and Mn–O bond lengths ranging from 1.8 to 2.2 Å, consistent with mixed-valent manganese centers bridged by oxygen atoms.^[16]^[17] These metrics reflect the cluster's compact yet asymmetric layout, where the calcium ion occupies a position that stabilizes the overall framework through coordination to the same oxygen bridges. The manganese ions adopt distorted octahedral coordination geometries, each ligated by six donors primarily consisting of oxygen atoms from the μ-oxo bridges and carboxylate side chains of protein residues like aspartate (Asp170, Asp342) and glutamate (Glu189, Glu333), supplemented by nitrogen from a histidine (His332) and water/hydroxide ligands.^[18] This environment ensures pseudocubane-like connectivity while allowing flexibility for redox changes. Early models based on X-ray data supported a high-oxidation paradigm for the S₁ state, with Mn valences of (III, IV, IV, III), implying shorter bond lengths due to higher electron density withdrawal.^[19] In contrast, low-oxidation paradigms proposed (II, III, III, IV), suggesting slightly elongated bonds to accommodate lower valences. Cryo-EM refinements in the 2020s, including structures at 1.95 Å resolution, have largely affirmed the distorted chair topology with refined ligand positions and reduced ambiguity in oxo bridge assignments, favoring interpretations closer to the high-oxidation model through better visualization of electron density around the Mn4Ca core.^[20]^[21]

Reaction Mechanism

The Kok Cycle

The Kok cycle delineates a four-step catalytic process in which the oxygen-evolving complex (OEC) of photosystem II progresses sequentially through oxidation states designated S₀, S₁, S₂, S₃, and a transient S₄ state, each advancement triggered by light-induced charge separation that oxidizes the OEC via the redox-active tyrosine residue Tyr_Z. This progression accumulates four oxidizing equivalents at the Mn₄CaO₅ cluster of the OEC, enabling the thermodynamically demanding four-electron oxidation of two water molecules to yield one O₂, four protons, and four electrons. The cycle resets to S₀ upon O₂ release from the S₄ state, ensuring sustained water-splitting activity during photosynthesis. Recent studies have further elucidated the S₃ → S₀ step, highlighting rate-determining roles of protein residues such as D61 in proton release and N298 in water insertion kinetics.^[22] Experimental observations of period-four oscillations in oxygen evolution and chlorophyll a fluorescence yield, elicited by trains of short saturating light flashes on dark-adapted samples, underpin the Kok cycle model. These oscillations reflect the probabilistic advancement through S-states, with maximal O₂ yield typically on the third flash when starting from the predominant dark-stable S₁ state, modulated by inefficiencies such as "misses" (failed oxidations) and "double hits" (extra advancements) that cause signal damping over successive cycles. Proton release occurs in a stoichiometric pattern tightly coupled to the S-state transitions: one H⁺ is released during the S₀ → S₁ and S₂ → S₃ steps, while two H⁺ are liberated in the S₃ → S₄ → S₀ transition alongside O₂ evolution, totaling four protons per full cycle to match the water oxidation stoichiometry. This pattern supports vectorial proton translocation into the thylakoid lumen, contributing to the photosynthetic proton motive force.^[23] Theoretical frameworks for the Kok cycle highlight proton-coupled electron transfer (PCET) mechanisms that maintain redox poise across states, mitigating the buildup of highly charged intermediates through concerted deprotonation events. Models propose that substrate water binding to the OEC integrates into this PCET scheme, particularly during the S₂ → S₃ transition, where a new water molecule may insert at the Mn₄CaO₅ cluster—potentially via nucleophilic attack or ligand exchange—to position the second substrate for eventual O-O bond formation in S₄.^[24]

S-State Transitions and Water Oxidation

The oxygen-evolving complex (OEC) undergoes a series of redox transitions through its S-states, each characterized by distinct oxidation states of the four manganese ions and structural rearrangements that build oxidizing equivalents for water splitting. In the S0 state, the Mn oxidation states are typically assigned as Mn(III)₃Mn(IV), representing the most reduced stable configuration after O₂ release.^[25] Upon photo-oxidation, the transition to S1 involves the loss of one electron, yielding Mn(III)₂Mn(IV)₂, with the resting dark-stable state being S1.^[26] The S1 to S2 advancement oxidizes one Mn(III) to Mn(IV), resulting in Mn(III)Mn(IV)₃, accompanied by proton release and subtle geometric changes in the Mn₄CaO₅ cluster.^[2] Further oxidation to S3 achieves the all-Mn(IV) configuration, Mn(IV)₄, which is thought to involve insertion or binding of a substrate water molecule, often associated with the oxo bridge O5 becoming more reactive.^[27] The S3 to S4 transition is transient and precedes O₂ formation, where S4 is proposed as a high-energy peroxo-like intermediate with an incipient O-O bond, potentially involving Mn(IV)-oxyl species or oxo radical character.^[28] Recent time-resolved serial femtosecond crystallography studies have illuminated the S1 to S2 dynamics, revealing a spin-state flip at Mn4 from low-spin (S=3/2) to high-spin (S=5/2), which facilitates electron transfer and cluster reorganization.^[2] Concurrently, the position of O5 shifts closer to Mn1 by approximately 0.3 Å, suggesting early substrate positioning for subsequent oxidation steps, while the overall cubane structure remains largely intact during this microsecond-scale process.^[2] The formation of the O-O bond, culminating in water oxidation, is debated but centers on two primary mechanisms in the S3/S4 regime. One involves oxo-oxyl radical coupling, where an oxo ligand (e.g., O5 as Mn(IV)=O) couples with an adjacent oxyl radical (Mn(IV)-O•) to form the peroxide bridge, supported by computational models showing low barriers for intramolecular radical recombination.^[28] An alternative proposes nucleophilic attack by a Ca²⁺-bound water or hydroxide on a high-valent Mn(V)=O species, generating the O-O bond through proton-coupled electron transfer, though this faces energetic challenges in certain cluster geometries.^[29] These mechanisms ensure efficient dioxygen release, restoring the S0 state and completing the cycle. Recent computational and experimental work (as of 2024) has proposed that S0 reformation involves rapid water insertion via Ca-bound waters, forming transient closed-cubane intermediates before achieving the open-cubane S0 configuration, with low-energy barriers facilitating the process.^[30] Kinetic studies indicate that S-state transitions occur on ultrafast to millisecond timescales, with the S0 to S1 step being the slowest at around 1-10 ms due to higher activation barriers in the reduced state.^[31] Subsequent transitions—S1 to S2 (~100 μs), S2 to S3 (~1 ms), and S3 to S0 (~1 ms)—proceed more rapidly, reflecting increasing redox potential.^[32] However, inefficiencies arise from "misses" (failed state advancement, ~5-20% per flash, often in S3 to S0) and "double-hits" (skipping a state, ~1-5%, more frequent in early transitions), which dampen the periodicity of O₂ evolution but are minimized under optimal conditions.^[33]

Historical Development

Early Discoveries

The initial insights into the oxygen-evolving complex (OEC) emerged from flash photolysis experiments in the 1960s, which demonstrated that oxygen production in photosynthesis follows a characteristic oscillatory pattern. In 1969, Pierre Joliot and his collaborators conducted experiments on dark-adapted spinach chloroplasts, illuminating them with short, saturating light flashes separated by dark intervals. They observed that oxygen evolution exhibited damped oscillations with a period of four flashes, peaking on the third, seventh, and eleventh flashes, indicating that four sequential photochemical turnovers are required to release one molecule of O₂ from water. Similar period-four oscillations were independently reported by Bessel Kok's group around the same time, using algae and isolated chloroplasts, further confirming the multi-step nature of the water-oxidation process.^[34] Building on these observations, Bessel Kok proposed the S-state model in 1970 to explain the oscillatory behavior. The model posits that the OEC accumulates four oxidizing equivalents through sequential light-induced charge separations, progressing through redox states S₀ to S₄, with O₂ release occurring upon reaching S₄ and spontaneous reversion to S₀. This framework was derived from the period-four pattern in flash-induced oxygen yields, accounting for "misses" (failed advancements) and "double hits" (skipped states) that cause damping. Although chlorophyll a fluorescence oscillations were also noted in related studies, Kok's formulation primarily addressed oxygen evolution kinetics. Early evidence for the involvement of manganese (Mn) in the OEC came from inhibition studies in the early 1970s. George Cheniae demonstrated that treatment with hydroxylamine (NH₂OH), a reductant, selectively depletes Mn from chloroplasts and abolishes oxygen evolution, while restoration of Mn partially recovers activity, establishing Mn's essential catalytic role. Similarly, 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of electron transfer between the primary and secondary quinone acceptors in photosystem II, allowed isolation of OEC function by blocking downstream electron flow without directly affecting water oxidation, highlighting the OEC's position upstream of the reaction center. By 1980, isotope-labeling experiments using ¹⁸O-enriched water provided key evidence that the water-splitting site is distinct from the photosystem II reaction center. Richard Radmer and Otto Ollinger monitored the oscillating ¹⁸O content in evolved O₂ during flash sequences, showing that the isotopic composition reflects two substrate water molecules incorporated per O₂ molecule, with no significant contribution from other cellular oxygen sources or the reaction center's redox components. This confirmed the OEC as a specialized enzymatic site for water oxidation, separate from the light-driven charge separation at P680.^[35]

Key Advances and Researchers

In the 1980s, electron paramagnetic resonance (EPR) spectroscopy provided critical evidence for the multinuclear manganese nature of the oxygen-evolving complex (OEC). Dismukes and Siderer observed a characteristic multiline EPR signal in the S₂ state of spinach chloroplasts, confirming the presence of a polynuclear Mn cluster involved in water oxidation. During the 1990s, X-ray absorption spectroscopy (XAS) and extended X-ray absorption fine structure (EXAFS) analyses advanced the structural characterization of the OEC. Yachandra, Klein, and Sauer utilized these techniques to determine short Mn-Mn distances of approximately 2.7 Å, supporting early models of a cubane-like Mn₄Ca cluster. A major breakthrough occurred in 2011 with the determination of the high-resolution crystal structure of photosystem II (PSII) at 1.9 Å resolution by Shen and Kamiya, which directly visualized the Mn₄CaO₅ cluster as a distorted cubane with an external Mn atom linked by oxo bridges. In the 2020s, structural studies have illuminated the dynamic nature of the OEC during catalytic cycles, building on the 2011 structure. Umena et al.'s foundational work enabled subsequent time-resolved analyses, while Suga et al. captured intermediate structures during S₁-to-S₂ and S₂-to-S₃ transitions, revealing conformational changes in the Mn₄CaO₅ cluster and surrounding residues that facilitate water oxidation.^[2] Parallel mechanistic insights have come from Brudvig, who integrated spectroscopic data to propose substrate binding pathways; Britt, whose pulsed EPR studies delineated spin states and ligand environments; and Renger, who developed theoretical frameworks for electron-proton coupling in the Kok cycle.^[36] Debates on O-O bond formation mechanisms, particularly oxo-oxyl radical versus nucleophilic attack pathways, were largely resolved through computational modeling in the 2000s. Siegbahn's density functional theory calculations favored an oxo-oxyl coupling mechanism in the S₄ state, with low energy barriers consistent with experimental kinetics.^[37]

Research Techniques

Spectroscopic Methods

Electron paramagnetic resonance (EPR) spectroscopy has been instrumental in characterizing the magnetic interactions within the Mn4CaO5 cluster of the oxygen-evolving complex (OEC) in photosystem II. In the S2 state, the OEC exhibits a characteristic g=2 multiline EPR signal, arising from hyperfine interactions between the unpaired electron spin and the four manganese ions, which indicates a multinuclear Mn cluster with antiferromagnetic coupling. This signal, observed at low temperatures, consists of approximately 20-25 hyperfine lines spaced by about 20-30 G, reflecting the nuclear spins of the Mn nuclei (I=5/2). Additionally, a broad g=4.1 signal appears in the S2 state, attributed to a spin S=5/2 ground state from a subset of the Mn ions, providing evidence for the mixed-valence configuration (Mn(III)Mn(IV)₃). X-ray absorption spectroscopy (XAS), including X-ray absorption near-edge structure (XANES) and extended X-ray absorption fine structure (EXAFS), probes the electronic structure and coordination environment of the Mn ions across S-states. XANES edge shifts during S-state transitions reveal changes in Mn oxidation states, with the Mn K-edge shifting to higher energies from S1 to S2 (indicating one Mn oxidation, e.g., Mn(III) to Mn(IV)) and further in higher states, supporting a progression such as (III,III,III,IV) in S0 to (III,IV,IV,IV) in S2.^[38] EXAFS analysis of Fourier transforms shows Mn-Mn distances of approximately 2.7 Å and 3.3 Å, corresponding to di-μ-oxo bridges and longer-range interactions in the cubane-like structure, with variations in bond lengths (e.g., shortening by ~0.1 Å upon S2 formation) that track the evolving geometry during catalysis.^[39] Fourier-transform infrared (FTIR) and Raman spectroscopies detect vibrational modes associated with the Mn-oxo core, offering insights into structural dynamics. In the S-states, characteristic bands in the 600-800 cm⁻¹ region correspond to asymmetric Mn-oxo-Mn stretching vibrations, with shifts such as the appearance of a ~610 cm⁻¹ mode in S2 (attributed to a Mn(IV)-O-Mn(III) unit) and further changes to ~650 cm⁻¹ in S3, indicating protonation or deprotonation events at bridging oxo ligands. Raman spectroscopy complements this by enhancing symmetric modes, revealing similar frequency ranges for Mn-O bonds and confirming the persistence of these vibrations through the Kok cycle, which helps distinguish between μ-oxo and hydroxo bridges.^[40] Time-resolved variants of these techniques, such as flash-induced EPR, capture kinetic aspects of S-state transitions and ligand identities. Flash photolysis followed by EPR detects the rapid formation of the S2 multiline signal within microseconds after the first flash, with lifetimes reflecting miss rates in the cycle (~10-20% per transition), and has been used to probe the role of O5, a key oxygen in the cluster. These experiments support O5 as a μ-oxo bridge in lower S-states, potentially converting to a hydroxo ligand in S3, based on hyperfine couplings and relaxation kinetics observed in ENDOR extensions of time-resolved EPR.

Crystallographic and Modeling Approaches

X-ray crystallography has been pivotal in elucidating the structure of the oxygen-evolving complex (OEC) within photosystem II (PSII), with resolutions progressively improving over time. The initial structure of PSII from Synechococcus elongatus was determined at 3.8 Å resolution in 2001, providing the first glimpse of the Mn4Ca cluster's overall arrangement but lacking atomic details. Subsequent refinements culminated in a 1.9 Å resolution structure in 2011, which clearly revealed the cubane-like topology of the OEC as a Mn3CaO4 cubane linked to a dangling Mn ion via an oxo bridge, enabling precise identification of ligand environments and metal-oxygen distances. These high-resolution maps confirmed the asymmetric coordination and supported the core's role in water oxidation. Serial femtosecond crystallography (SFX), often combined with cryo-electron microscopy (cryo-EM) techniques, has advanced the capture of transient S-state intermediates in the OEC. In 2024, pump-probe SFX experiments on PSII from Thermosynechococcus vestitus achieved room-temperature snapshots from nanoseconds to milliseconds post-illumination, resolving structural dynamics during the S1-to-S2 transition, including subtle shifts in Mn-Mn distances and water ligand rearrangements. These time-resolved structures complement earlier cryo-EM maps of PSII megacomplexes at ~3 Å resolution, which integrate the OEC within the full protein assembly but with less emphasis on catalytic intermediates. Quantum mechanical/molecular mechanics (QM/MM) modeling has provided mechanistic insights into OEC function by simulating electronic and geometric changes during catalysis. Using density functional theory within QM/MM frameworks, these models optimize the Mn4CaO5 cluster's geometry in various S-states, predicting Mn oxidation states and protonation patterns that align with experimental bond lengths. A key proposal from such calculations is the oxyl radical coupling mechanism for O-O bond formation in the S4 state, where a Mn(IV)-oxyl species couples with a bridging oxo, lowering the energy barrier for dioxygen release compared to nucleophilic attack pathways. Synthetic mimics of the OEC, particularly cubane clusters, serve as benchmarks for validating structural and functional models derived from crystallography and simulations. The [Mn4O4]6+ core, synthesized in 1999 as a molecular mimic, exhibits reversible four-electron redox chemistry and light-driven O2 evolution, mirroring the native cluster's cuboidal motif and oxidation potential. More advanced heterometallic analogs, such as the [Mn4CaO4]6+ cluster reported in 2015, replicate the Mn3CaO4 subsite with similar spectroscopic signatures and stepwise oxidation, aiding in testing proposed OEC geometries and reaction coordinates.

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Structures and Energetics for O2 Formation in Photosystem II
Oct 26, 2009 · The oxygen evolving complex (OEC), the complex within PSII that catalyzes the actual formation of the O−O bond, contains four manganese atoms ...
[35]
X-ray Absorption Spectroscopy on Layered Photosystem II ...
We propose that photosynthetic oxygen evolution involves cycling of the photosystem II manganese complex through four distinct oxidation states.Missing: seminal | Show results with:seminal
[36]
Vibrational spectroscopy of the oxygen-evolving complex and of ...
In this communication, we have reviewed the current progress on the application of FTIR spectroscopy in both the mid-IR and low-frequency regions to study the ...Missing: seminal papers