PubMed1994
Oxygenic photosystem (PS) II complex from spinach photooxidized hydroxyurea (HU) to produce its aminoxy radical, which was identified by its electron spin resonance spectrum. HU was apparently photooxidized by the water-oxidizing enzyme (WOE) since the photooxidation reaction was blocked by carbonyl cyanide m-chlorophenylhydrazone (CCCP). HU radicals photoproduced by the WOE inhibited the electron transfer between the redox-active tyrosine residue (YZ), which is involved in electron transfer from the WOE to the reaction center chlorophyll of PS II, and the secondary quinone electron acceptor. Treatment of PS II complex with Tris resulted in the appearance of a CCCP-insensitive photooxidation site for HU. Photoproduced HU radicals in oxygenic and Tris-treated PS II complex decayed with first-order kinetics, an indication that the radicals reacted primarily with surrounding molecules rather than decayed through spontaneous dismutation or recombination. HU inhibited the diphenylcarbazide-supported photoreduction of 2,6-dichlorophenolindophenol (DCIP) in Tris-treated PS II complex preincubated only under illumination, but this inhibition was suppressed when ascorbate was added to scavenge HU radicals. If examined in darkness, HU radicals could not, however, inhibit subsequent photoreduction of DCIP. Therefore, the photoproduced HU radicals interact with a photogenerated site(s) in the PS II complex. The photoproduction of YZ., a radical of YZ, was suppressed to about 40% in Tris-treated PS II complex by the in situ-photogenerated HU radicals, and the yield of a cation radical of chlorophyll, close to the PS II reaction center, was increased, while the production of a radical of another redox-active tyrosine residue in PS II (YD.) was hardly affected.(ABSTRACT TRUNCATED AT 250 WORDS)