The mechanism for proton-coupled electron transfer from tyrosine in a model complex and comparisons with Y-z oxidation in photosystem II

QC 20100525
In the water-oxidizing reactions of photosystem II (PSII), a tyrosine residue plays a key part as an intermediate electron-transfer reactant between the primary donor chlorophylls (the pigment P-680) and the water-oxidizing Mn cluster. The tyrosine is deprotonated upon oxidation, and the coupling between the proton reaction and electron transfer is of great mechanistic importance for the understanding of the water-oxidation mechanism. Within a programme on artificial photosynthesis, we have made and studied the proton-coupled tyrosine oxidation in a model system and been able to draw mechanistic conclusions that we use to interpret the analogous reactions in PSII.

Styring, StenbjörnLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biok-sst (författare)
Akermark, B. (författare)
Sun, Licheng C. (författare)
Biokemi och StrukturbiologiCentrum för Molekylär Proteinvetenskap (creator_code:org_t)

Ingår i:Philosophical Transactions of the Royal Society of London. Biological Sciences: The Royal Society357:1426, s. 1471-14780962-84361471-2970

Av författaren/redakt...: Sjodin, M.; Styring, Stenbjö ...; Akermark, B.; Sun, Licheng C.

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