Mössbauer studies of the non‐heme iron and cytochrome b 559 in a Chlamydomonas reinhardtii PSI− mutant and their interactions with α‐tocopherol quinone

FEBS Letters

Strzaka, Kazimierz²  Kruse, Olaf³  Schmid, Georg H.³  Borgstädt, Rüdiger³  Burda, Květoslava¹  Stanek, Jan⁴  Kruk, Jerzy² 

[1] Institute of Nuclear Physics, ul. Radzikowskiego 152, 31-342 Cracow, Poland;Faculty of Biotechnology, Jagiellonian University, al. Mickiewicza 3, 31-120 Cracow, Poland;Lehrstuhl Zellphysiologie, Fakultät für Biologie, Universität Bielefeld, Postfach 10 01 31, D-33501 Bielefeld, Germany;Institute of Physics, Jagiellonian University, ul. Reymonta 4, 31-059 Cracow, Poland

关键词: Photosystem II;    Non-heme iron;    Cytochrome b 559;    α-Tocopherol quinone;    α-TQ;    α-tocopherol quinone;    FCCP;    carbonylcyanide-p-trifluoromethoxy-phenyl-hydrazone;    δ;    isomer shift;    ΔE;    quadrupole splitting;    HP;    high potential;    LP;    low potential;   

DOI  :  10.1016/S0014-5793(02)03895-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Fe³⁺ state. A possible role of the non-heme iron and α-TQ in electron flow through the PSII is discussed.

【 授权许可】

Unknown