Bacteria photosynthetic electron

In contrast to common usage, the distinction between photosynthetic and respiratory Rieske proteins does not seem to make sense. The mitochondrial Rieske protein is closely related to that of photosynthetic purple bacteria, which represent the endosymbiotic ancestors of mitochondria (for a review, see also (99)). Moreover, during its evolution Rieske s protein appears to have existed prior to photosynthesis (100, 101), and the photosynthetic chain was probably built around a preexisting cytochrome be complex (99). The evolution of Rieske proteins from photosynthetic electron transport chains is therefore intricately intertwined with that of respiration, and a discussion of the photosynthetic representatives necessarily has to include excursions into nonphotosynthetic systems. 

Photosynthetic bacteria have relatively simple phototransduction machinery, with one of two general types of reaction center. One type (found in purple bacteria) passes electrons through pheophytin (chlorophyll lacking the central Mg2+ ion) to a quinone. The other (in green sulfur bacteria) passes electrons through a quinone to an iron-sulfur center. Cyanobacteria and plants have two photosystems (PSI, PSII), one of each type, acting in tandem. Biochemical and biophysical... 

Another nonheme Mn center is believed [172] to be present in photosynthetic green filamentous bacteria. The locus of the Mn ion in these bacteria is similar to that of the nonheme Fe11 in photosynthetic purple bacteria [173], i.e., between two quinones, along the pathway of electron transfer. Since the Fe center of purple bacteria does not seem to be involved directly in the electron transfer process (i.e., is not redox-active), the redox role of the Mn analog remains in question. This Mn may be redox-active, considering that (1) structural differences between the purple and green bacteria photosynthetic apparatus do exist [173] and (2) the green bacteria display different functionalities, such as C02 fixation, which does not occur via the classical Calvin or reverse Krebs cycle [174],... 

Smeda et al. (1993) reported that in a mutation of the psb A gene in a photoautotropic potato, atrazine resistance was attributable to a mutation from AGT (ser) to ACT (threonine) in codon 264 of the psb A gene that encodes the Qb protein. Although the mutant cells exhibited extreme levels of resistance to atrazine, no concomitant reductions in photosynthetic electron transport or cell growth rates were detected compared to the unselected cells. This is in contrast with the losses in productivity observed in atrazine-resistant mutants that contain a Ser to Gly 264 alteration. Research has shown that triazine resistance by various algae and photosynthetic bacteria has been due to changes in many different binding sites (Oettmeier, 1999). 

Table I also shows the great diversity of organisms in which iron—sulfur proteins have been detected. Thus far there is no organism which when appropriately examined has not contained an iron-sulfur protein, either in the soluble or membrane-bound form. Iron-sulfur proteins catalyze reactions of physiological importance in obligate anaerobic bacteria, such as hydrogen uptake and evolution, ATP formation, pyruvate metabolism, nitrogen fixation, and photosynthetic electron transport. These properties and reactions can be considered primitive and thus make iron-sulfur proteins a good place to start the study of evolution. These key reactions are also important in higher organisms. Other reactions catalyzed by iron-sulfur proteins can be added such as hydroxylation, nitrate and nitrite reduction, sulfite reduction, NADH oxidation, xanthine oxidation, and many other reactions (Table II).

Nonetheless, photosynthesis did not evolve immediately at the origin of life. The failure to discover photosynthesis in the domain of Archaea implies that photosynthesis evolved exclusively in the domain of Bacteria. Eukaryotes appropriated through endosymbiosis the basic photosynthetic units that were the products of bacterial evolution. All domains of life do have electron-transport chains in common, however. As we have seen, components such as the ubiquinone-cytochrome c oxidoreductase and cytochrome hf family are present in both respiratory and photosynthetic electron-transport chains. These components were the foundations on which light-energy-capturing systems evolved. 

In purple photosynthetic bacteria, and specifically in Rps. sphaeroides and Rps. capsulata, three cytochromes of b type have been identified by means of redox titration, in the dark, of isolated chromatophores [116]. They are characterized by midpoint potentials at pH = 7.0 equal to 0.155, 0.050 and -0.090 V (in Rps. sphaeroides)-, the of the 0.050 V species is pH dependent ( — 60 mV per pH unit) [116,117]. The presence of a cytochrome cc in these organisms, interfering spectrally with cytochrome b, makes the situation unclear as far as the existence of cyt. b E j = 0.155 V) is concerned [118]. The two other cytochromes E = 0.050 and — 0.090 V) have also been resolved kinetically in studies on the photosynthetic electron transport and on the basis of their spectral characteristics (band at 561 nm and a spht bands at 558 and 556 nm, respectively these two cytochromes will be referred to as 6-561 and 6-566 in the following) [119]. 

A band with a molecular weight of 25 000 of the bacterial oxidoreductase has been identified with the high-potential Fe-S protein, by means of cross reaction with a monospecific antibody against the analogous electron carrier from Neurospora crassa mitochondria. The existence of this type of Fe-S center in photosynthetic bacteria was first discovered by ESR spectroscopy [125] and its involvement in photosynthetic electron transport was demonstrated. The midpoint potential in Rps. sphaeroides is 0.285 V, and is pH dependent above pH 8, with a decrease of 60 mV per pH unit [125]. 

The latter process was shown to require ATP, but the source of this ATP was unclear and a matter of considerable dispute. The breakthrough came in 1954 when Arnon and his colleagues demonstrated light-induced ATP synthesis in isolated chloroplasts. The same year Frenkel described photophosphorylation in cell-free preparations from bacteria. Photophosphorylation in both chloroplasts and bacteria was found to be associated with membranes, in the former case with the thylakoid membrane and in the latter with structures derived from the plasma membrane, called chromatophores. In the following years work in a number of laboratories, including those of Arnon, Avron, Chance, Duysens, Hill, Jagendorf, Kamen, Kok, San Pietro, Trebst, Witt and others, resulted in the identification and characterization of various catalytic components of photosynthetic electron transport. Chloroplasts and bacteria were also shown to contain ATPases similar to the F,-ATPase of mitochondria. 

Bacterial copper proteins are found only in the plasma membrane (Gram-positive bacteria) or in the plasma membrane and the periplasm (Gram-negative bacteria), not in the bacterial cytoplasm. However, cyanobacteria do have copper proteins in their cytoplasm. These important photosynthetic bacteria require copper for plastocyanin, which plays a critical role in the photosynthetic electron transport chain. Both plastocyanin and cytochrome c oxidase are found in the thylakoid compartments within the cytoplasm. In Synechocystis, the Cu(I) Pie-ATPase CtaA imports Cu(I). A second ATPase, PacS, imports Cu(I) into the thylakoid, and the Atxl-like copper chaperone ScAtxl is believed to deliver Cu(I) from CtaA to PacS (Fig. 8.6). 

A functionally similar but structurally much simpler version of the bc complex is found in the plasma membrane of many bacteria, where it participates among other processes in respiration, denitrification, nitrogen fixation, and cyclic photosynthetic electron transfer. 

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