Photosynthesis reaction center

Figure 12.1. Schematic diagram of a photosynthesis reaction center. Light is absorbed by pigments in the light-gathering antenna and absorbed energy is transferred to a photochemically active site P, where it is utilized to initiate photosynthetic reactions.

Porphyrin-quinone compounds as models of photosynthesis reaction center 89UK1032. 

Nakamura et al. demonstrated direct detection of herbicides by using a heavy-subunit-histidine-tagged photosynthesis reaction center (HHisRC) from bacterium Rhodobacter sphaerodies [26] (Fig. 3). They used a Biacore X instrument (from Biacore AB, Sweden) and a sensor chip with dextran matrix... 

Deisenhofer J and Michel H (1989) The photosynthesis reaction center from the bacterium Rhodopseudomonas viridis. EMBO 18 2149-2170... 

Yruela I, Alfonso M, Ortiz de Zarate I et al. Precise location of the Cu(II)-inhibitory binding site in higher plant and bacterial photosynthesis reaction centers as probed by light-induced absorption changes. J Biol Chem 1993 268(3) 1684-1689. 

Total Structure and Function of a Complete Photosynthesis Reaction Center... 

While nanotechnology is a recent human discovery, Namre has been at it for nearly 4 bilHon years in s) tems described earlier in the present book. The ubiquitous conversion of ADP to ATP for storage of metabolic energy occurs through a biological nanomotor called ATP synthase. Another example is the membrane-embedded photosynthesis reaction center of purple baaeria. The ribosome is a highly structured machine that constructs proteins firom amino acids from a blueprint and its detailed, atomic-level structure is described later in this chapter. 

Both PSI and PSII are necessary for photosynthesis, but the systems do not operate in the implied temporal sequence. There is also considerable pooling of electrons in intermediates between the two photosystems, and the indicated photoacts seldom occur in unison. The terms PSI and PSII have come to represent two distinct, but interacting reaction centers in photosynthetic membranes (36,37) the two centers are considered in combination with the proteins and electron-transfer processes specific to the separate centers. 

Despite considerable efforts very few membrane proteins have yielded crystals that diffract x-rays to high resolution. In fact, only about a dozen such proteins are currently known, among which are porins (which are outer membrane proteins from bacteria), the enzymes cytochrome c oxidase and prostaglandin synthase, and the light-harvesting complexes and photosynthetic reaction centers involved in photosynthesis. In contrast, many other membrane proteins have yielded small crystals that diffract poorly, or not at all, using conventional x-ray sources. However, using the most advanced synchrotron sources (see Chapter 18) it is now possible to determine x-ray structures from protein crystals as small as 20 pm wide which will permit more membrane protein structures to be elucidated. 

While this electron flow takes place, the cytochrome on the periplasmic side donates an electron to the special pair and thereby neutralizes it. Then the entire process occurs again another photon strikes the special pair, and another electron travels the same route from the special pair on the periplasmic side of the membrane to the quinone, Qb, on the cytosolic side, which now carries two extra electrons. This quinone is then released from the reaction center to participate in later stages of photosynthesis. The special pair is again neutralized by an electron from the cytochrome. 

What molecular architecture couples the absorption of light energy to rapid electron-transfer events, in turn coupling these e transfers to proton translocations so that ATP synthesis is possible Part of the answer to this question lies in the membrane-associated nature of the photosystems. Membrane proteins have been difficult to study due to their insolubility in the usual aqueous solvents employed in protein biochemistry. A major breakthrough occurred in 1984 when Johann Deisenhofer, Hartmut Michel, and Robert Huber reported the first X-ray crystallographic analysis of a membrane protein. To the great benefit of photosynthesis research, this protein was the reaction center from the photosynthetic purple bacterium Rhodopseudomonas viridis. This research earned these three scientists the 1984 Nobel Prize in chemistry. 

The quantum yield of photosynthesis, the amount of product formed per equivalent of light input, has traditionally been expressed as the ratio of COg fixed or Og evolved per quantum absorbed. At each reaction center, one photon or quantum yields one electron. Interestingly, an overall stoichiometry of one translocated into the thylakoid vesicle for each photon has also been observed. Two photons per center would allow a pair of electrons to flow from HgO to NADP (Figure 22.12), resulting in the formation of 1 NADPH and Og. If one ATP were formed for every 3 H translocated during photosynthetic electron transport, 1 ATP would be synthesized. More appropriately, 4 hv per center (8 quanta total) would drive the evolution of 1 Og, the reduction of 2 NADP, and the phosphorylation of 2 ATP. 

Studies (see, e.g., (101)) indicate that photosynthesis originated after the development of respiratory electron transfer pathways (99, 143). The photosynthetic reaction center, in this scenario, would have been created in order to enhance the efficiency of the already existing electron transport chains, that is, by adding a light-driven cycle around the cytochrome be complex. The Rieske protein as the key subunit in cytochrome be complexes would in this picture have contributed the first iron-sulfur center involved in photosynthetic mechanisms (since on the basis of the present data, it seems likely to us that the first photosynthetic RC resembled RCII, i.e., was devoid of iron—sulfur clusters). 

It is interesting to compare the thermal-treatment effect on the secondary structure of two proteins, namely, bacteriorhodopsin (BR) and photosynthetic reaction centers from Rhodopseudomonas viridis (RC). The investigation was done for three types of samples for each object-solution, LB film, and self-assembled film. Both proteins are membrane ones and are objects of numerous studies, for they play a key role in photosynthesis, providing a light-induced charge transfer through membranes—electrons in the case of RC and protons in the case of BR. 

Carotenoids protect photosynthetic organisms against potentially harmful photooxidative processes and are essential structural components of the photosynthetic antenna and reaction center complexes. Plant carotenoids play fundamental roles as accessory pigments for photosynthesis, as protection against photooxidation, and... 

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