At least eleven thylakoid proteins become phosphorylated under reducing conditions, and redox titration has identified a common midpoint potential of Em = +38 +/- 4 mV, n = 0.95 +/- 0.06. In the presence of the phosphatase inhibitor NaF (10 mM), the redox dependency of phosphorylation is found to be essentially unchanged: Em = +50 +/- 3 mV, n = 1.02 +/- 0.04. Thylakoid membranes were phosphoryl...

Chemical redox reactions have been exploited to transform unreactive vinylferrocene into a powerful dienophile for the Diels-Alder reaction and reactive substrate for thiol addition reactions upon conversion to its ferrocenium state. We have further investigated the ability of these reactions to facilitate redox-auxiliary-like reactivity by further hydrogenolyisis of the Diels-Alder adduct to t...

Reduction-oxidation (redox) reactions are an essential part of cell metabolism and represent a major fraction of all catabolic and anabolic reactions. Their dominant characteristic is that they generate and consume compounds with in part highly negative redox potential. Redox reactions occur at many sites in the cell, e.g. in membranes such as thylakoids, plastid envelope, and plasma membrane a...

Reduction-oxidation (redox) reactions are an essential part of cell metabolism and represent a major fraction of all catabolic and anabolic reactions. Their dominant characteristic is that they generate and consume compounds with in part highly negative redox potential. Redox reactions occur at many sites in the cell, e.g. in membranes such as thylakoids, plastid envelope, and plasma membrane a...

The redox status of the cell is described by the ratio of reduced to non-reduced compounds. Redox reactions which determine the redox state are an essential feature of all living beings on Earth. However, the first life forms evolved under strongly anoxic conditions of the young Earth, and the redox status probably was based on iron and sulphur compounds. Nowadays, redox reactions in cells have...

Model reactions offer a chemical mechanism by which formation of a sulfenyl amide residue at the active site of the redox-regulated protein tyrosine phosphatase PTP1B protects the cysteine redox switch in this enzyme against irreversible oxidative destruction. The results suggest that 'overoxidation' of the sulfenyl amide redox switch to the sulfinyl amide in proteins is a chemically reversible...

Photosynthesis consists of a series of reactions catalyzed by redox enzymes to synthesize carbohydrates using solar energy. In order to take the advantage of solar energy, many researchers have investigated artificial photosynthesis systems mimicking the natural photosynthetic enzymatic redox reactions. These redox reactions usually require cofactors, which due to their high cost become a key i...

The biosynthetic pathways of most alcohols are linked to intracellular redox homeostasis, which is crucial for life. This crucial balance is primarily controlled by the generation of reducing equivalents, as well as the (reduction)-oxidation metabolic cycle and the thiol redox homeostasis system. As a main oxidation pathway of reducing equivalents, the biosynthesis of most alcohols includes red...

Recent advances in the coordination chemistry studies of the redox-interconverted ligands NO, NO and NO(HNO), particularly related to the pentacyanoferrate(II) and (III) fragments, are summarized with mention of structural, spectroscopic (IR and EPR) and DFT calculations. The chemistry of bound NO is presented with an emphasis on the mechanisms of the nucleophilic addition reactions of OH, amin...