Inhibition of the water oxidizing complex of photosystem II and the reoxidation of the quinone acceptor QA- by Pb2+.

The action of the environmental toxic Pb(2+) on photosynthetic electron transport was studied in thylakoid membranes isolated from spinach leaves. Fluorescence and thermoluminescence techniques were performed in order to determine the mode of Pb(2+) action in photosystem II (PSII). The invariance of fluorescence characteristics of chlorophyll a (Chl a) and magnesium tetraphenylporphyrin (MgTPP), a molecule structurally analogous to Chl a, in the presence of Pb(2+) confirms that Pb cation does not interact directly with chlorophyll molecules in PSII.

Alteration of the structure and function of photosystem I by Pb2+.

The toxic effects of Pb(2+) on photosynthetic electron transport were studied in photosystem I (PSI) submembrane fractions isolated from spinach. Structural and spectroscopic analysis using FTIR, fluorescence and X-ray photoelectron spectroscopy (XPS) showed that Pb(2+) binds with proteins via oxygen and nitrogen atoms with an overall binding constant of KPb-PSI=4.9×10(3) (±0.

Re-evaluation of the side effects of cytochrome b6f inhibitor dibromothymoquinone on photosystem II excitation and electron transfer.

Dibromothymoquinone (DBMIB) has been used as a specific inhibitor of plastoquinol oxidation at the Q0 binding site of the cytochrome b6f complex for 40 years. It is thought to suppress electron transfer between photosystem (PS) II and I, as well as cyclic electron transfer around PSI. However, DBMIB has also been reported to act as a quencher of chlorophyll excited states.

Locating the binding sites of retinol and retinoic acid with milk β-lactoglobulin.

β-lactoglobulin (β-LG) is a member of lipocalin superfamily of transporters for small hydrophobic molecules such as retinoids. We located the binding sites of retinol and retinoic acid on β-LG in aqueous solution at physiological conditions, using FTIR, CD, fluorescence spectroscopic methods, and molecular modeling. The retinoid-binding sites and the binding constants as well as the effect of retinol and retinoic acid complexation on protein stability and secondary structure were determined.

Locating the binding sites of Pb(II) ion with human and bovine serum albumins.

Lead is a potent environmental toxin that has accumulated above its natural level as a result of human activity. Pb cation shows major affinity towards protein complexation and it has been used as modulator of protein-membrane interactions. We located the binding sites of Pb(II) with human serum (HSA) and bovine serum albumins (BSA) at physiological conditions, using constant protein concentration and various Pb contents.