| 1. |
- Blomberg, Margareta R A, et al.
(författare)
-
A Quantum Chemical Study of Hydrogen Abstraction from Manganese-Coordinated Water by a Tyrosyl Radical: A Model for Water Oxidation in Photosystem II
- 1997
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 119:35, s. 8285-8292
-
Tidskriftsartikel (refereegranskat)abstract
- Recently, water oxidation in photosystem II was proposed to involve direct abstraction of hydrogen atoms from water molecules terminally ligated to manganese ions in the oxygen-evolving complex by the oxidized tyrosine radical, TyrZ. This model is tested here by performing quantum chemical calculations. An empirically parametrized hybrid density functional method is used, and both monomeric and dimeric manganese model systems are studied. It is found that, by coordination to a manganese center, the first O-H bond strength of water is lowered from 113.4 to 84.3 kcal/mol. This O-H bond strength is only 2.8 kcal/mol stronger than that in tyrosine. Using an extended basis set, we find that this difference decreases still further. The second hydrogen abstraction energy is quite similar. Since thermoneutrality in the reaction (or a weak exothermicity) is a requirement for the hydrogen abstraction model, the present calculations support this model. Possible functions of a coordinated chloride and a nearby calcium complex are suggested. Five- or six-coordination and ferro- or antiferromagnetic spin couplings of the manganese centers are discussed.
|
|
| 2. |
- Borgström, Magnus, et al.
(författare)
-
Light induced manganese oxidation and long-lived charge separation in a Mn-2(II,II)-Ru-II (bpy)(3)-acceptor triad
- 2005
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 127:49, s. 17504-17515
-
Tidskriftsartikel (refereegranskat)abstract
- The photoinduced electron-transfer reactions in a Mn-2(II.II)-R-II-NDI triad (1) ([Mn-2(bpmp)(OAc)(2)](+), bpmp = 2,6-bis[bis(2-pyridylmethyl)aminomethyl]-4-methyiphenolate and OAc = acetate, R-II = trisbipyridine ruthenium(II), and NDI = naphthalenediimide) have been studied by time-resolved optical and EPR spectroscopy. Complex 1 is the first synthetically linked electron donor-sensitizer-acceptor triad in which a manganese complex plays the role of the donor. EPR spectroscopy was used to directly demonstrate the light induced formation of both products: the oxidized manganese dimer complex (Mn-2(II.III)) and the reduced naphthalenediimide (NDIcenter dot-) acceptor moieties, while optical spectroscopy was used to follow the kinetic evolution of the [Ru(bpy)(3)](2+) intermediate states and the NDIcenter dot- radical in a wide temperature range. The average lifetime of the NDI- radical is ca. 600 mu s at room temperature, which is at least 2 orders of magnitude longer than that for previously reported triads based on a [Ru(bpy)(3)](2+) photosensitizer. At 140 K, this intramolecular recombination was dramatically slowed, displaying a lifetime of 0.1-1 s, which is comparable to many of the naturally occurring charge-separated states in photosynthetic reaction centra. It was found that the long recombination lifetime could be explained by an unusually large reorganization energy (lambda approximate to 2.0 eV), due to a large inner reorganization of the manganese complex. This makes the recombination reaction strongly activated despite the large driving force (-Delta G degrees = 1.07 eV). Thus, the intrinsic properties of the manganese complex are favorable for creating a long-lived charge separation in the "Marcus normal region" also when the charge separated state energy is high.
|
|
| 3. |
- Magnuson, Ann, et al.
(författare)
-
A Biomimetic Model System for the Water Oxidizing Triad in Photosystem II
- 1999
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 121:1, s. 89-96
-
Tidskriftsartikel (refereegranskat)abstract
- In plants, solar energy is used to extract electrons from water, producing atmospheric oxygen. This is conducted by Photosystem II, where a redox ”triad” consisting of chlorophyll, a tyrosine, and a manganese cluster, governs an essential part of the process. Photooxidation of the chlorophylls produces electron transfer from the tyrosine, which forms a radical. The radical and the manganese cluster together extract electrons from water, providing the biosphere with an unlimited electron source. As a partial model for this system we constructed a ruthenium(II) complex with a covalently attached tyrosine, where the photooxidized ruthenium was rereduced by the tyrosine. In this study we show that the tyrosyl radical, which gives a transient EPR signal under illumination, can oxidize a manganese complex. The dinuclear manganese complex, which initially is in the Mn(III)/(III) state, is oxidized by the photogenerated tyrosyl radical to the Mn(III)/(IV) state. The redox potentials in our system are comparable to those in Photosystem II. Thus, our synthetic redox “triad” mimics important elements in the electron donor ”triad” in Photosystem II, significantly advancing the development of systems for artificial photosynthesis based on ruthenium−manganese complexes.
|
|
| 4. |
- Magnuson, Ann, et al.
(författare)
-
Mimicking electron transfer reactions in photosystem II : synthesis and photochemical characterization of a ruthenium(II) tris(bipyridyl) complex with a covalently linked tyrosine.
- 1997
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 119:44, s. 10720-10725
-
Tidskriftsartikel (refereegranskat)abstract
- In the natural photosynthetic reaction center photosystem II, absorption of a photon leads to photooxidationof the primary electron donor P680, which subsequently retrieves electrons from a tyrosyl residue, functioning as aninterface to the oxygen-evolving manganese complex. In a first step toward mimicking these reactions, we havemade a Ru(II)-polypyridine complex with an attached tyrosyl moiety. The photoexcited ruthenium complex playedthe role of P680and was first oxidized by external acceptors. Combined transient absorbance and EPR studies provided evidence that the Ru(III) formed was reduced by intramolecular electron transfer from the attached tyrosine, with a rate constant of 5104s-1. Thus we show that a tyrosine radical could be formed by light-induced electrontransfer reactions, and we indicate future directions for developing a closer analogy with the photosystem II reactions.
|
|
| 5. |
- Sjodin, M., et al.
(författare)
-
Proton-coupled electron transfer from tyrosine in a tyrosine-ruthenium-tris-bipyridine complex : Comparison with Tyrosine(z) oxidation in photosystem II
- 2000
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 122:16, s. 3932-3936
-
Tidskriftsartikel (refereegranskat)abstract
- The pH- and the temperature dependence of the rate constant for electron transfer from tyrosine to ruthenium in Ru(II)(bpy)(2)(4-Me-4'CONH-L-tyrosine etyl ester-2,2'-bpy) 2PF(6) was investigated using flash photolysis. At a pH below the tyrosine pK(a) approximate to 10 the rate constant increased monotonically with pH. This increase was consistent with a concerted electron transfer/deprotonation mechanism. Also indicative of a concerted reaction was the unusually high reorganization energy, 2 eV, extracted from temperature-dependent measurements. Deprotonation of the tyrosine group, at pH > pK(a), resulted in a 100-fold increase in rate constant due to a decreased reorganization energy, lambda = 0.9 eV. Also, the rate constant became independent of pH, In Mn-depleted photosystem II a similar pH dependence has been found for electron transfer from tyrosine(Z) (Tyr(Z)) to the oxidized primary donor P680(+). On the basis of the kinetic similarities we propose that the mechanisms in the two systems are the same, that is, the electron transfer occurs as a concerted proton-coupled electron-transfer reaction, and at pH < 7 the Tyr(Z) proton is released directly to the bulk water.
|
|
| 6. |
- Sjödin, Martin, et al.
(författare)
-
Switching the redox mechanism : Models for proton coupled electron transfer from tyrosine and tryptophan
- 2005
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 127:11, s. 3855-3863
-
Tidskriftsartikel (refereegranskat)abstract
- The coupling of electron and proton transfer is an important controlling factor in radical proteins, such as photosystem II, ribinucleotide reductase, cytochrome oxidases, and DNA photolyase. This was investigated in model complexes in which a tyrosine or tryptophan residue was oxidized by a laser-flash generated trisbipyridine-Ru-III moiety in an intramolecular, proton-coupled electron transfer (PCET) reaction. The PCET was found to proceed in a competition between a stepwise reaction, in which electron transfer is followed by deprotonation of the amino acid radical (ETPT), and a concerted reaction, in which both the electron and proton are transferred in a single reaction step (CEP). Moreover, we found that we could analyze the kinetic data for PCET by Marcus' theory for electron transfer. By altering the solution pH, the strength of the Ru-III oxidant, or the identity of the amino acid, we could induce a switch between the two mechanisms and obtain quantitative data for the parameters that control which one will dominate. The characteristic pH-dependence of the CEP rate (M. Sjodin et al. J. Am. Chem. Soc. 2000, 122, 3932) reflects the pH-dependence of the driving force caused by proton release to the bulk. For the pH-independent ETPT on the other hand, the driving force of the rate-determining ET step is pH-independent and smaller. On the other hand, temperature-dependent data showed that the reorganization energy was higher for CEP, while the pre-exponential factors showed no significant difference between the mechanisms. Thus, the opposing effect of the differences in driving force and reorganization energy determines which of the mechanisms will dominate. Our results show that a concerted mechanism is in general quite likely and provides a low-barrier reaction pathway for weakly exoergonic reactions. In addition, the kinetic isotope effect was much higher for CEP (k(H)/k(D) > 10) than for ETPT (k(H)/k(D) = 2), consistent with significant changes along the proton reaction coordinate in the rate-determining step of CEP.
|
|
| 7. |
- Sun, L C, et al.
(författare)
-
Binuclear ruthenium-manganese complexes as simple artificial models for photosystem II in green plants
- 1997
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 119:30, s. 6996-7004
-
Tidskriftsartikel (refereegranskat)abstract
- As part of a project aimed at developing models for photosystem II (PSII) in green plants, we have prepared a series of model compounds (7, 8, and 13). In these compounds, a photosensitizer, ruthenium(II) tris(bipyridyl) complex (to mimic the function of P-680 in PSII), was covalently linked to a manganese(II) ion through different bridging ligands. The structures of the compounds were characterized by electron paramagnetic resonance measurements and electrospray ionization mass spectrometry. The interaction between the ruthenium and manganese moieties within the complex was probed by steady-state and time-resolved emission measurements. When the binuclear complexes are exposed to flash photolysis in the presence of an electron acceptor such as methylviologen (MV2+), it could be shown that after the initial electron transfer from the excited state of Ru(II) in compound 7, forming Ru(III) and MV+., an intramolecular electron transfer from coordinated Mn(II) to the photogenerated Ru(III) occurred with a first-order rate constant of 1.8 x 10(5) s(-1), regenerating Ru(II). This is believed to be the first supramolecular system where a manganese complex has been used as an electron donor to a photo-oxidized photosensitizer, Possible extensions to develop the manganese donor, and thus to approach the function of reaction center in PSII, are indicated.
|
|
| 8. |
- Sun, Licheng, et al.
(författare)
-
Hydrogen-Bond Promoted Intramolecular Electron Transfer to Photogenerated Ru(III): A Functional Mimic of TyrosineZ and Histidine 190 in Photosystem II
- 1999
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 121:29, s. 6834-6842
-
Tidskriftsartikel (refereegranskat)abstract
- As a model for redox components on the donor side of photosystem II (PS II) in green plants, a supramolecular complex 4 has been prepared. In this, a ruthenium(II) tris-bipyridyl complex which mimics the function of P680 in PS II, has been covalently linked to a tyrosine unit which bears two hydrogen-bonding substituents, dipicolylamine (dpa) ligands. Our aim is to mimic the interaction between tyrosineZ and a basic histidine residue, namely His190 in PSII, and also to use the dpa ligands for coordination of manganese. Two different routes for the synthesis of the compound 4 are presented. Its structure was fully characterized by 1H NMR, COSY, NOESY, 13C NMR, IR, and mass spectrometry. 1H NMR and NOESY gave evidence for the existence of intramolecular hydrogen bonding in 4. The interaction between the ruthenium and the substituted tyrosine unit was probed by steady-state and time-resolved emission measurements as well as by chemical oxidation. Flash photolysis and EPR measurements on 4 in the presence of an electron acceptor (methylviologen, MV2+, or cobalt pentaminechloride, Co3+) showed that an intermolecular electron transfer from the excited state of Ru(II) in 4 to the electron acceptor took place, forming Ru(III) and the methylviologen radical MV+ or Co2+. This was followed by intramolecular electron transfer from the substituted tyrosine moiety to the photogenerated Ru(III), regenerating Ru(II) and forming a tyrosyl radical. In water, the radical has a g value of 2.0044, indicative of a deprotonated tyrosyl radical. In acetonitrile, a radical with a g value of 2.0029 was formed, which can be assigned to the tyrosine radical cation. In both solvents the electron transfer is intramolecular with a rate constant kET > 1 × 107 s-1. This is 2 orders of magnitude greater than the one for a similar compound 3, in which no dpa arm is attached to the tyrosine unit. Therefore the hydrogen bonding between the substituted tyrosine and the dpa arms in 4 is proposed to be responsible for the fast electron transfer. This interaction mimics the proposed His190 and tyrosineZ interaction in the donor side of PS II.
|
|
| 9. |
- Tommos, Cecilia, et al.
(författare)
-
Stepwise Disintegration of the Photosynthetic Oxygen-Evolving Complex
- 1998
-
Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 1520-5126 .- 0002-7863. ; 120:40, s. 10441-10452
-
Tidskriftsartikel (refereegranskat)abstract
- Photosynthetic water oxidation catalyzed by Photosystem II takes place at a site that comprises a redox-active tyrosine, YZ, a tetramanganese cluster, and, in addition to its redox components, two inorganic cofactors, calcium and chloride. Recent work suggests that YZ and the metal site are intimately linked in the oxidation and deprotonation reactions of substrate water. The metal cluster stores oxidizing equivalents and provides binding sites for the substrate from which YZ is proposed to abstract hydrogen atoms during the catalytic cycle of photosystem II. Intrinsic to this hydrogen-abstraction mechanism for water oxidation is an intimate structural and functional relationship between the metal site and YZ, which predicts that the local YZ environment will be sensitive to the composition and integrity of the metal cluster. To test this postulate, we have examined the YZ site and its status with respect to solvent exposure under varying degrees of disassembly of the oxygen-evolving complex. 1H2H-isotope exchange was carried out for various times in samples devoid of Mn, Ca2+, and Cl-, and in samples depleted exclusively of Ca2+. The YZ and S2YZ species were cryotrapped to high yield in these two preparations, respectively, and the radical site was characterized by using electron spin-echo envelope modulation spectroscopy. The isotope exchange at the YZ site was completed with an upper limit on the minutes time scale in both the (Mn)4-depleted and the Ca-depleted samples. The number of isotope-exchangeable protons in the site and their distances to YZ were found to be different in the two systems, indicating that YZ is shielded from the solvent in the Ca-depleted system and, upon removal of the (Mn)4 cluster, becomes accessible to bulk water. The results from an electron spin-echo analysis of S2YZ, in the weak-coupling limit, suggest that YZ in samples that retain the (Mn)4 cluster, but lack Ca2+, is involved in a bifurcated hydrogen bond. The data for both classes of samples are consistent with a hydrogen-abstraction function for YZ in water oxidation and provide insight into the light-driven assembly of the (Mn)4 cluster.
|
|
