Mössbauer Studies of Cu(II) Ions Interaction with the Non-Heme Iron and Cytochrome b_{559} in a Chlamydomonas reinhardtii PSI Minus Mutant

• Authors: K Burda , J Kruk , K Strzałka , J Stanek , G Schmid , O Kruse
• Languages of publication: EN

Abstracts

EN

Mössbauer spectroscopy was applied, for the first time, to study the interaction of copper ions with the non-heme iron and the heme iron of cytochrome b_{559} in photosystem II thylakoids isolated from a Chlamydomonas reinhardtii photosystem I minus mutant. We showed that copper ions oxidize the heme iron and change its low spin state into a high spin state. This is probably due to deprotonation of the histidine coordinating the heme. We also found that copper preserves the non-heme iron in a low spin ferrous state, enhancing the covalence of iron bonds as compared to the untreated sample. We suggest that a disruption of hydrogen bonds stabilizing the quinone-iron complex by Cu^{2+} is the mechanism responsible for a new arrangement of the binding site of the non-heme iron leading to its more "tense" structure. Such a diamagnetic state of the non-heme iron induced by copper results in a magnetic decoupling of iron from the primary quinone acceptor. These results indicate that Cu does not cause removal of the non-heme iron from its binding site. The observed Cu^{2+} action on the non-heme iron and cytochrome b_{559} is similar to that previously observed forα-tocopherol quinone.

Keywords

EN

82.39.Jn; 82.39.Rt; 82.50.Nd; 87.15.He; 87.64.Pj; 89.60.Fe

Discipline

• 82.39.Rt: Reactions in complex biological systems(see also 87.18.-h Biological complexity)
• 89.60.Fe: Environmental regulations(see also 01.78.+p Science and government)
• 82.39.Jn: Charge (electron, proton) transfer in biological systems
• 82.50.Nd: Control of photochemical reactions

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2006
• Volume: 109
• Issue: 3
• Pages: 237-247

Dates

published

2006-03

received

2005-05-20

Contributors

author

K Burda

• Institute of Physics, Jagiellonian University, Reymonta 4, 30-059 Kraków, Poland
• Institute of Nuclear Physics, Polish Academy of Sciences, Radzikowskiego 152, 31-342 Krakó Poland

author

J Kruk

• Faculty of Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland

author

K Strzałka

• Faculty of Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland

author

J Stanek

• Institute of Physics, Jagiellonian University, Reymonta 4, 30-059 Kraków, Poland

author

G Schmid

• University of Bielefeld, Department of Biology, Molecular Cell Physiology, Universitaetsstr. 25, 33501 Bielefeld, Germany

author

O Kruse

• University of Bielefeld, Department of Biology, Molecular Cell Physiology, Universitaetsstr. 25, 33501 Bielefeld, Germany

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Identifiers

DOI

10.12693/APhysPolA.109.237