TY - JOUR
T1 - EPR-ENDOR characterization of ( 17O, 1H, 2H) water in manganese catalase and its relevance to the oxygen-evolving complex of photosystem II
AU - McConnell, Iain L.
AU - Grigoryants, Vladimir M.
AU - Scholes, Charles P.
AU - Myers, William K.
AU - Chen, Ping Yu
AU - Whittaker, James W.
AU - Brudvig, Gary W.
PY - 2012/1/25
Y1 - 2012/1/25
N2 - The synthesis of efficient water-oxidation catalysts demands insight into the only known, naturally occurring water-oxidation catalyst, the oxygen-evolving complex (OEC) of photosystem II (PSII). Understanding the water oxidation mechanism requires knowledge of where and when substrate water binds to the OEC. Mn catalase in its Mn(III)-Mn(IV) state is a protein model of the OEC's S 2 state. From 17O-labeled water exchanged into the di-μ-oxo di-Mn(III,IV) coordination sphere of Mn catalase, CW Q-band ENDOR spectroscopy revealed two distinctly different 17O signals incorporated in distinctly different time regimes. First, a signal appearing after 2 h of 17O exchange was detected with a 13.0 MHz hyperfine coupling. From similarity in the time scale of isotope incorporation and in the 17O μ-oxo hyperfine coupling of the di-μ-oxo di-Mn(III,IV) bipyridine model (Usov, O. M.; Grigoryants, V. M.; Tagore, R.; Brudvig, G. W.; Scholes, C. P.J. Am. Chem. Soc. 2007, 129, 11886-11887), this signal was assigned to μ-oxo oxygen. EPR line broadening was obvious from this 17O μ-oxo species. Earlier exchange proceeded on the minute or faster time scale into a non-μ-oxo position, from which 17O ENDOR showed a smaller 3.8 MHz hyperfine coupling and possible quadrupole splittings, indicating a terminal water of Mn(III). Exchangeable proton/deuteron hyperfine couplings, consistent with terminal water ligation to Mn(III), also appeared. Q-band CW ENDOR from the S 2 state of the OEC was obtained following multihour 17O exchange, which showed a 17O hyperfine signal with a 11 MHz hyperfine coupling, tentatively assigned as μ-oxo- 17O by resemblance to the μ-oxo signals from Mn catalase and the di-μ-oxo di-Mn(III,IV) bipyridine model.
AB - The synthesis of efficient water-oxidation catalysts demands insight into the only known, naturally occurring water-oxidation catalyst, the oxygen-evolving complex (OEC) of photosystem II (PSII). Understanding the water oxidation mechanism requires knowledge of where and when substrate water binds to the OEC. Mn catalase in its Mn(III)-Mn(IV) state is a protein model of the OEC's S 2 state. From 17O-labeled water exchanged into the di-μ-oxo di-Mn(III,IV) coordination sphere of Mn catalase, CW Q-band ENDOR spectroscopy revealed two distinctly different 17O signals incorporated in distinctly different time regimes. First, a signal appearing after 2 h of 17O exchange was detected with a 13.0 MHz hyperfine coupling. From similarity in the time scale of isotope incorporation and in the 17O μ-oxo hyperfine coupling of the di-μ-oxo di-Mn(III,IV) bipyridine model (Usov, O. M.; Grigoryants, V. M.; Tagore, R.; Brudvig, G. W.; Scholes, C. P.J. Am. Chem. Soc. 2007, 129, 11886-11887), this signal was assigned to μ-oxo oxygen. EPR line broadening was obvious from this 17O μ-oxo species. Earlier exchange proceeded on the minute or faster time scale into a non-μ-oxo position, from which 17O ENDOR showed a smaller 3.8 MHz hyperfine coupling and possible quadrupole splittings, indicating a terminal water of Mn(III). Exchangeable proton/deuteron hyperfine couplings, consistent with terminal water ligation to Mn(III), also appeared. Q-band CW ENDOR from the S 2 state of the OEC was obtained following multihour 17O exchange, which showed a 17O hyperfine signal with a 11 MHz hyperfine coupling, tentatively assigned as μ-oxo- 17O by resemblance to the μ-oxo signals from Mn catalase and the di-μ-oxo di-Mn(III,IV) bipyridine model.
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U2 - 10.1021/ja203465y
DO - 10.1021/ja203465y
M3 - Article
C2 - 22142421
AN - SCOPUS:84863393528
SN - 0002-7863
VL - 134
SP - 1504
EP - 1512
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 3
ER -