The preparation of Dl/D2/cytochrome 6559 complex isolated from pea (Pisum sativum h.) was photoinactivated by "white light" (140 W m‘2) at 20 and 4 "C in both the presence and absence of oxygen. The inactivation was followed by measuring the decline of the photoinduced absorbance change A/4683 (the photoaccumulation of reduced pheophytin), by measuring absorption spectra and fluorescence emission, and by polypeptide analysis. In the presence of oxygen, the ability of the DUDUcyi 6559 complex to acciunulate reduced pheophytin was lost with the halftime im of about 3 min and fluorescence quantum yield declined with ti/2 of about 30 min at both 20 and 4 ^C. The D\ and Dl polypeptides were rapidly modified at 20 °C as reflected by the presence of their large aggregates at the start of the electrophoretic gel and by a decrease of the mobility of remaining Dl and Dl monomers. This modification was substantially limited at 4 “C. Subímits of cytochrome 6559 were not modified at any temperature. When oxygen was removed, the halftime of the A/1683 decline increased by about one order of magnitude, fluorescence emission did not decline, but slightly increased, and the polypeptide pattem was only slightly affected during irradiation.