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EPR-ENDOR characterization of (17O, 1H, 2H) water in manganese catalase and its relevance to the oxygen-evolving complex of photosystem II.

ABSTRACT: 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 (17)O-labeled water exchanged into the di-?-oxo di-Mn(III,IV) coordination sphere of Mn catalase, CW Q-band ENDOR spectroscopy revealed two distinctly different (17)O signals incorporated in distinctly different time regimes. First, a signal appearing after 2 h of (17)O exchange was detected with a 13.0 MHz hyperfine coupling. From similarity in the time scale of isotope incorporation and in the (17)O ?-oxo hyperfine coupling of the di-?-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 ?-oxo oxygen. EPR line broadening was obvious from this (17)O ?-oxo species. Earlier exchange proceeded on the minute or faster time scale into a non-?-oxo position, from which (17)O 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 (17)O exchange, which showed a (17)O hyperfine signal with a 11 MHz hyperfine coupling, tentatively assigned as ?-oxo-(17)O by resemblance to the ?-oxo signals from Mn catalase and the di-?-oxo di-Mn(III,IV) bipyridine model.

SUBMITTER: McConnell IL

PROVIDER: S-EPMC3471538 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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EPR-ENDOR characterization of (17O, 1H, 2H) water in manganese catalase and its relevance to the oxygen-evolving complex of photosystem II.

McConnell Iain L IL Grigoryants Vladimir M VM Scholes Charles P CP Myers William K WK Chen Ping-Yu PY Whittaker James W JW Brudvig Gary W GW

Journal of the American Chemical Society 20120109 3

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 (17)O-labeled water exchanged into the di-μ-oxo di-Mn(III,IV) coordination sphere of Mn catalase, CW ...[more]

PMID: 22142421

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Project description:Carotenoids are indispensable molecules for life. They are present everywhere in plants, algae, bacteria whom they protect against free radicals and oxidative stress. Through the consumption of fruits and vegetables and some carotenoid-containing fish, they are introduced into the human body and, similarly, protect it. There are numerous health benefits associated with the consumption of carotenoids. Carotenoids are antioxidants but at the same time they are prone to oxidation themselves. Electron loss from the carotenoid forms a radical cation. Furthermore, proton loss from a radical cation forms a neutral radical. In this mini-review, we discuss carotenoid radicals studied in our groups by various physicochemical methods, namely the radical cations formed by electron transfer and neutral radicals formed by proton loss from the radical cations. They contain many similar hyperfine couplings due to interactions between the electron spin and numerous protons in the carotenoid. Different EPR and ENDOR methods in combination with DFT calculations have been used to distinguish the two independent carotenoid radical species. DFT predicted larger coupling constants for the neutral radical compared to the radical cation. Previously, INDO calculations miss assigned the large couplings to the radical cation. EPR and ENDOR have aided in elucidating the physisorb, electron and proton transfer processes that occur when carotenoids are adsorbed on solid artificial matrices, and predicted similar reactions in aqueous solution or in plants. After years of study of the physicochemical properties of carotenoid radicals, the different published results start to merge together for a better understanding of carotenoid radical species and their implication in biological systems. Up until 2008, the radical chemistry in artificial systems was elucidated but the correlation between quenching ability and neutral radical formation was an inspiration to look for these radical species in vivo. In addition, the EPR spin-trapping technique has been applied to study inclusion complexes of carotenoids with different delivery systems.

Dataset Information

EPR-ENDOR characterization of (17O, 1H, 2H) water in manganese catalase and its relevance to the oxygen-evolving complex of photosystem II.

Publications

EPR-ENDOR characterization of (17O, 1H, 2H) water in manganese catalase and its relevance to the oxygen-evolving complex of photosystem II.

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