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Mössbauer studies of the non‐heme iron and cytochrome b 559 in a Chlamydomonas reinhardtii PSI − mutant and their interactions with α‐tocopherol quinone
Author(s) -
Burda Květoslava,
Kruk Jerzy,
Borgstädt Rüdiger,
Stanek Jan,
Strza Kazimierz,
Schmid Georg H.,
Kruse Olaf
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03895-4
Subject(s) - chlamydomonas reinhardtii , heme , chemistry , photochemistry , cytochrome , cofactor , hemeprotein , crystallography , mutant , biochemistry , gene , enzyme
Spin and valence states of the non‐heme iron and the heme iron of cytochrome b 559 , as well as their interactions with α‐tocopherol quinone (α‐TQ) in photosystem II (PSII) thylakoid membranes prepared from the Chlamydomonas reinhardtii PSI − mutant have been studied using Mössbauer 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 α‐TQ does not change the spin and the valence states of the non‐heme iron but enhances the covalence of its bonds. α‐TQ oxidizes the heme iron into the high spin Fe 3+ state. A possible role of the non‐heme iron and α‐TQ in electron flow through the PSII is discussed.