Hydrogen-bond promoted intramolecular electron transfer to photogenerated Ru(III): A functional mimic of Tyrosine(Z) and histidine 190 in photosystemII
Lc. Sun et al., Hydrogen-bond promoted intramolecular electron transfer to photogenerated Ru(III): A functional mimic of Tyrosine(Z) and histidine 190 in photosystemII, J AM CHEM S, 121(29), 1999, pp. 6834-6842
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 P-680 in
PS II, has been covalently linked to a tyrosine unit which bears two hydrog
en-bonding substituents, dipicolylamine (dpa) ligands. Our aim is to mimic
the interaction between tyrosine(Z) and a basic histidine residue, namely H
is190 in PSII, and also to use the dpa ligands for coordination of manganes
e. Two different routes for the synthesis of the compound 4 are presented.
Its structure was fully characterized by H-1 NMR, COSY, NOESY,C-13 NMR, LR,
and mass spectrometry. H-1 NMR and NOESY gave evidence for the existence o
f intramolecular hydrogen bonding in 4. The interaction between the rutheni
um and the substituted tyrosine unit was probed by steady-state and time-re
solved emission measurements as well as by chemical oxidation. Flash photol
ysis and EPR measurements on 4 in the presence of an electron acceptor (met
hylviologen, MV2+, Or cobalt pentaminechloride, Co3+) showed that an interm
olecular electron transfer from the excited state of Ru(II) in 4 to the ele
ctron acceptor took place, forming Ru(III) and the methylviologen radical M
V+. or Co2+. This was followed by intramolecular electron transfer from the
substituted tyrosine moiety to the photogenerated Ru(III), regenerating Ru
(Il) 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 ra
dical with a g value of 2.0029 was formed, which can be assigned to the tyr
osine radical cation. In both solvents the electron transfer is intramolecu
lar with a rate constant k(ET) > 1 x 10(7) S-1 This is 2 orders of magnitud
e greater than the one for a similar compound 3, in which no dpa arm is att
ached to the tyrosine unit. Therefore the hydrogen bonding between the subs
tituted tyrosine and the dpa arms in 4 is proposed to be responsible for th
e fast electron transfer. This interaction mimics the proposed His190 and t
yrosine(Z) interaction in the donor side of PS II.