JXB Advance Access originally published online on May 12, 2006
Journal of Experimental Botany 2006 57(8):1809-1816; doi:10.1093/jxb/erj189
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RESEARCH PAPER |
Photoinhibition of manganese enzymes: insights into the mechanism of photosystem II photoinhibition
Department of Plant Physiology and Molecular Biology, University of Turku, 20014 University of Turku, Finland
*To whom correspondence should be addressed. E-mail: esatyy{at}utu.fi
Evidence has recently been presented that photoinhibition of photosystem II (PSII) is triggered by absorption of light by the oxygen-evolving manganese cluster. To get insight into the effects of light on enzymes containing manganese or other transition metal cofactors, the photosensitivities of Mn catalase, Mn superoxide dismutase, the haem (Fe)-containing bovine liver catalase, and CuZn superoxide dismutase were investigated. Glucose oxidase was studied as an example of an enzyme that does not have a metal cofactor. Sensitivities of these five enzymes to UVC, UVA, and visible light were compared in anaerobic conditions. The Mn(III)-oxo-Mn(III)-containing Mn catalase was found to be more sensitive to both visible and UV light than bovine liver catalase. Furthermore, the action spectrum of photoinhibition of Mn catalase was found to be fairly similar to that of photoinhibition of PSII. The Mn(II)-containing Mn superoxide dismutase was sensitive to UVC light and somewhat sensitive to UVA light, while only UVC light caused some inhibition of CuZn superoxide dismutase. Glucose oxidase was the least photosensitive of the enzymes studied. The photosensitivity of Mn enzymes supports the hypothesis that the oxygen-evolving manganese complex of PSII can be damaged by UV and visible light absorbed by its Mn(III) or Mn(IV) ions.
Key words: Action spectrum, bovine liver catalase, glucose oxidase, manganese catalase, oxygen-evolving complex, photodynamic damage, photoinhibition, PSII, superoxide dismutase
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