Miguel Ángel De La Rosa

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The reaction mechanism of electron transfer from the interchangeable metalloproteins plastocyanin (Pc) and cytochrome c6 (Cyt) to photooxidized P700 in photosystem I (PSI) has been studied by laser-flash absorption spectroscopy using a number of evolutionarily differentiated organisms such as cyanobacteria (Anabaena sp. PCC 7119 and Synechocystis sp. PCC(More)
BACKGROUND Electron transfer between cytochrome f and photosystem I (PSI) can be accomplished by the heme-containing protein cytochrome c6 or by the copper-containing protein plastocyanin. Higher plants use plastocyanin as the only electron donor to PSI, whereas most green algae and cyanobacteria can use either, with similar kinetics, depending on the(More)
Photosynthesis consists of a series of endergonic redox reactions, with light as the source of energy, chlorophyll as the energy converter, and electrons flowing through membrane and soluble proteins. Here, we give an account of the most recent results on the structure-function relationships of the membrane-embedded complexes cytochrome b(6)-f and(More)
A comparative thermodynamic analysis of photosystem I (PSI) reduction by plastocyanin (Pc) and cytochrome c6 (Cyt) has been carried out by laser-flash absorption spectroscopy in the cyanobacteria Anabaena PCC 7119 and Synechocystis PCC 6803 as well as in spinach. These three organisms have been reported to exhibit different reaction mechanisms [Hervas, M.,(More)
Laser-flash absorption spectroscopy has been used to investigate the kinetics of electron transfer from reduced cytochrome c6 and plastocyanin, isolated from Anabaena PCC 7119, to oxidized P700 in photosystem-I particles isolated from the same cyanobacterium and from spinach. For all metalloproteins and photosystems, the observed rate constant has a(More)
Plastocyanin and cytochrome c6 from the green alga Monoraphidium braunii reduce the photo-oxidized algal photosystem I (PSI) reaction center chlorophyll (P700) with similar kinetics, as expected from their functional equivalence. The observed P700+ reduction rate constants show a non-linear dependence on metalloprotein concentration, which indicates a(More)
A soluble low-potential cytochrome c549 has been purified in milligram quantities from the cyanobacterium Synechocystis sp. PCC 6803. The protein exhibits an acid isoelectric point of 3.9, a molecular mass of 15.8 kDa, and a midpoint redox potential value of -250 mV at pH 7.0 EPR and 1H NMR studies suggest a low-spin heme iron with bis-histidine(More)
A soluble monoheme c-type cytochrome (cytochrome c6) has been isolated from the green alga Monoraphidium braunii. It has a molecular mass of 9.3 kDa, an isoelectric point of 3.6 and a reduction potential of 358 mV at pH 7. The determined amino acid sequence allows its classification as a class-I c-type cytochrome. The ferric and ferrous cytochrome forms and(More)
The genes coding for plastocyanin (petE) and cytochrome c6 (petJ) from Anabaena sp. PCC 7119 have been cloned and properly expressed in Escherichia coli. The recombinant proteins are identical to those purified from the cyanobacterial cells. The products of both the petE and petJ genes are correctly processed in E. coli, as deduced from their identical(More)
Oxidation of the soluble, truncated form of cytochrome f by wild-type and mutant species of plastocyanin has been analyzed by laser flash absorption spectroscopy in the cyanobacterium Nostoc (formerly, Anabaena) sp. PCC 7119. At low ionic strengths, the apparent electron transfer rate constant of cytochrome f oxidation by wild-type plastocyanin is 1.34 x(More)