Photo synthetic bacteria

NapB. NapB is a subunit of the heterodimeric periplasmic nitrate reductase (NapAB) and transfers electrons to the catalytic NapA molybdoprotein. Nap systems are found in a number of bacteria, iucluding enterobacteria, aerobic denitrifiers, and nonsulfur purple photo synthetic bacteria. Their physiological function is different in these groups of bacteria and includes redox balancing using nitrate as an electron sink to dispose of excess rednctant, aerobic denitrification, and nitrate scavenging in nitrate-limited environments. 

B. Chance, H. Schleyer, and V. Legallais, Studies on Microalgae and Photo-synthetic Bacteria (Japanese Society of Plant Physiology, ed.), p. 337. Univ. of Tokyo Press, Tokyo, 1963. 

Brune, D., 1995. Sulfur compormds and photosynthetic electron donors. In Blakeship, R., Madigan, M., Bauer, C. (Eds.), Anoxygerric Photo-Synthetic Bacteria. Kluwer Academic PubUshers, Boston, pp. 847—870. 

The purple bacteria are perhaps not all anaerobic, and might be regarded as an ancestral form of the aerobic photo synthetic bacteria (APB) (Beatty, 2002). 

Fig. 1. (a) Schematic representation of the three types of anoxygenic ([1] and [2]) and oxygenic ([3]) photosynthesis found in plants and bacteria, (b) Phylogenetic tree based on 16S-rRNA sequence comparisons featuring only photo synthetic phyla. 

Michel, H. and J. Deisenhofer (1988). Relevance of the photo synthetic reaction center from purple bacteria to the structure of photosystem II. Biochemistry, 27 1-7. 

Figure 7 Rogue s gallery of structures of peripheral anteima complexes. As labelled these include Chlorosomes from green sulfur bacteria, fused antenna domains of the Photosystem I core, the CP43 and CP47 proteins of Photosystem II, the Fenna-Matthew-Olson (FMO) protein associated with chlorosomes, LHI proteins surrounding a purple bacterial photo synthetic core, the peridinin-chlorophyll a protein of dinoflagellate algae, the LHCI and LHCII proteins found in plants and many algae, and the LHII protein complex that is associated with LHI in purple bacteria...

Carbon dioxide is also fixed in the dark by photosynthetic organisms by the so-called Wood-Werkman reaction (Wood and Stjemholm, 1962). The CO2 assimilated, however, rarely exceeds that formed by dark respiration i.e. there is no net CO2 uptake. On the other hand, the amount of organic carbon derived from CO2 may be as high as 30% in heterotrophic bacteria and 90% in mixotrophic organisms. In the natural environment, non-photo-synthetic CO2 fixation by these organisms, together with the above-mentioned dark fixation by photosynthetic organisms, may under some condi-... 

Photosynthetic bacteria such as Rhodopseudomonas viridis contain a photo-synthetic reaction center that has been revealed at atomic resolution. The bacterial reaction center consists of four polypeptides L (31 kd), M (36 kd), and H (28 kd) subunits and C, a c-type cytochrome with four c-type hemes (figure 19.9). Sequence comparisons and low-resolution structural studies have rmaled that the bacterial reaction center is homologous to the more complex plant systems. Thus, many of our observations of the bacterial system will apply to plant systems as well. 

Decoloring. Much attention is now given to proteins from photo-synthetic origin (88), especially those from blue-green algae (89), nonsulfur purple bacteria (90), and green leaves (91), as possible food protein sources. These proteins contain large amounts of photosynthetic... 

Fritzsch G, Ermler U, Merckel M and Michel H (1996) Crystallization and structure of the photo synthetic reaction centres from Rhodobacter sphaeroides—wild type and mutants. In Michel-Beyerle M-E (ed) Reaction Centers of Photosynthetic Bacteria. Structure and Dynamics, pp 3-13. Springer-Verlag, Berlin... 

J. L. Martin, J. Breton, J. C. Lambry, and G. Fleming. The primary electron transfer in photosynthetic purple bacteria Long range electron transfer in the femtosecond domain at low temperature. In J. Breton and A. Vermeglio, editors. The Photo synthetic Bacterial Reaction Center Structure and Dynamics, pages 195-203, New York and London, 1988. Plenum Press. 

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