The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Proton-Coupled Electron Transfer from Tyrosine in a Tyrosine−Ruthenium−tris-Bipyridine Complex: Comparison with TyrosineZ Oxidation in Photosystem II
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 p K a ≈ 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 > p K a, resulted in a 100-fold increase in rate constant due to a decreased reorganization energy, λ = 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.
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Electron transfers in chemistry and biology
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PROTON-COUPLED ELECTRON TRANSFER: A Reaction Chemist's View
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Self-citationSolvent Effects on the Rates and Mechanisms of Reaction of Phenols with Free Radicals
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The Possible Role of Proton‐Coupled Electron Transfer (PCET) in Water Oxidation by Photosystem II
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Self-citationProton-Coupled Electron Transfer in Solution, Proteins, and Electrochemistry
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Metadata
- Authors
- Sjödin, M., Styring, S., Åkermark, B., Sun, L., & Hammarström, L.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-04-01
- Volume
- 122
- Issue
- 16
- Pages
- 3932-3936
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1995067163
- Cited by
- 265
- References
- 6
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- closed
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