Mössbauer studies of the non‐heme iron and cytochrome b559 in a Chlamydomonas reinhardtii PSI− mutant and their interactions with α‐tocopherol quinone

Spin and valence states of the non-heme iron and the heme iron of cytochrome b(559), as well as their interactions with a-tocopherol quinone (alpha-TQ) in photosystem II (PSII) thylakoid membranes prepared from the Chlamydomonas reinhardtii PS1(-) mutant have been studied using Mossbauer spectroscopy. Both of the iron atoms are in low spin ferrous states. The Debye temperature of the non-heme is 194 K and of the heme iron is 182 K. The treatment of alpha-TQ does not change the spin and the valence states of the non-heme iron but enhances the covalence of its bonds. alpha-TQ oxidizes the heme iron into the high spin Fe3+ state. A possible role of the non-heme iron and alpha-TQ in electron flow through the PSII is discussed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.