A common ancestor for oxygenic and anoxygenic photosynthetic systems

Schubert, Wolf‐Dieter; Klukas, Olaf; Saenger, Wolfram; Witt, H. T.; Fromme, Petra; Krauß, Norbert

doi:10.1006/jmbi.1998.1824

Cited by 235 publications

(75 citation statements)

References 69 publications

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“…The mutations in PsaA and PsaB were designed by using the crystal structures of PS I and the related purple bacterial reaction center as a guide (2,6,22). The structural data on PS I suggested that the most likely region for binding the phylloquinones was the stretch of highly conserved residues in PsaA and PsaB forming the stromal ␣-helices n and nЈ (2).…”

Section: Resultsmentioning

confidence: 99%

“…3) and the fact that the bacterial type I reaction centers are homodimers (4,5), the possibility of two parallel electron transfer pathways up to F X should be considered. However, based on the structural analogies of the core of PS I to the purple bacteria reaction center, which suggested a common evolutionary origin for all photosynthetic reaction centers (6), it has been generally thought that electron transport in PS I is unidirectional, as it is in the type II reaction centers. Most data supporting this view comes from electron paramagnetic resonance (EPR) experiments, in which only a single quinone anion radical can be accumulated during strong illumination under reducing conditions sufficient to reduce the terminal acceptors (7,8) (although see ref.…”

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confidence: 99%

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Evidence for two active branches for electron transfer in photosystem I

Guergova-Kuras

Boudreaux

Joliot

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

323

288

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All photosynthetic reaction centers share a common structural theme. Two related, integral membrane polypeptides sequester electron transfer cofactors into two quasi-symmetrical branches, each of which incorporates a quinone. In type II reaction centers [photosystem (PS) II and proteobacterial reaction centers], electron transfer proceeds down only one of the branches, and the mobile quinone on the other branch is used as a terminal acceptor. PS I uses iron-sulfur clusters as terminal acceptors, and the quinone serves only as an intermediary in electron transfer. Much effort has been devoted to understanding the unidirectionality of electron transport in type II reaction centers, and it was widely thought that PS I would share this feature. We have tested this idea by examining in vivo kinetics of electron transfer from the quinone in mutant PS I reaction centers. This transfer is associated with two kinetic components, and we show that mutation of a residue near the quinone in one branch specifically affects the faster component, while the corresponding mutation in the other branch specifically affects the slower component. We conclude that both electron transfer branches in PS I are active.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Evidence for two active branches for electron transfer in photosystem I

Guergova-Kuras

Boudreaux

Joliot

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

323

288

View full text Add to dashboard Cite

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“…As detailed above, in the case of the D1 protein, the C-terminal domain together with the loop joining transmembrane helices C and D contains most of amino acids that constitute the OEC. The structural relationship between the L/M and D1/D2 proteins also carries over to the C-terminal domains of the reactioncentre proteins of photosystem I (PSI) and almost certainly to that of the strictly anaerobic green sulphur photosynthetic bacteria despite the fact these type I RCs have a FeS centre as their terminal electron acceptor (Rhee et al 1998;Schubert et al 1998;. Therefore, there is no doubt that the reaction centres of all types of photosynthetic organisms present today evolved from a common ancestor.…”

Section: Evolutionary Origin Of Psii and The Oecmentioning

confidence: 99%

“…Again, there is a remarkable structural similarity between them and the PSI reaction-centre proteins, this time at their N-terminus (Rhee et al 1998;Schubert et al 1998;; see figure 5). As shown in figure 6a, the most striking difference being the presence of the large loop joining helices V and VI in the case of the PSII proteins, which for CP43 contains amino acids, that makes up a part of the OEC as mentioned above.…”

Section: (B) Inner Light-harvesting Systemsmentioning

confidence: 99%

Photosynthetic generation of oxygen

Barber

2008

Phil. Trans. R. Soc. B

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The oxygen in the atmosphere is derived from light-driven oxidation of water at a catalytic centre contained within a multi-subunit enzyme known as photosystem II (PSII). PSII is located in the photosynthetic membranes of plants, algae and cyanobacteria and its oxygen-evolving centre (OEC) consists of four manganese ions and a calcium ion surrounded by a highly conserved protein environment. Recently, the structure of PSII was elucidated by X-ray crystallography thus revealing details of the molecular architecture of the OEC. This structural information, coupled with an extensive knowledge base derived from a wide range of biophysical, biochemical and molecular biological studies, has provided a framework for understanding the chemistry of photosynthetic oxygen generation as well as opening up debate about its evolutionary origin.

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“…X-ray and electron diffraction data on PSI (FeS type) and PSII (Fe-quinone type) reaction center complexes and numerous phylogenetic analyses of the core reaction center proteins from cyanobacteria and higher plants reveal that they have several striking structural similarities in common, both with each other and also with type II purple bacterial reaction centers (7,8). These similarities support the long-standing hypothesis of a common evolutionary origin for all reaction center complexes, despite the large sequence divergence of type I (FeS-type) and type II (Fe-quinone type) reaction center genes (5, 9, 10).…”

Section: Genomic and Pigment Evidence For A Reaction Centermentioning

confidence: 99%

The origin of atmospheric oxygen on Earth: The innovation of oxygenic photosynthesis

Dismukes

Klimov

Baranov

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

325

240

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The evolution of O2-producing cyanobacteria that use water as terminal reductant transformed Earth's atmosphere to one suitable for the evolution of aerobic metabolism and complex life. The innovation of water oxidation freed photosynthesis to invade new environments and visibly changed the face of the Earth. We offer a new hypothesis for how this process evolved, which identifies two critical roles for carbon dioxide in the Archean period. First, we present a thermodynamic analysis showing that bicarbonate (formed by dissolution of CO 2) is a more efficient alternative substrate than water for O 2 production by oxygenic phototrophs. This analysis clarifies the origin of the long debated ''bicarbonate effect'' on photosynthetic O 2 production. We propose that bicarbonate was the thermodynamically preferred reductant before water in the evolution of oxygenic photosynthesis. Second, we have examined the speciation of manganese(II) and bicarbonate in water, and find that they form Mnbicarbonate clusters as the major species under conditions that model the chemistry of the Archean sea. These clusters have been found to be highly efficient precursors for the assembly of the tetramanganese-oxide core of the water-oxidizing enzyme during biogenesis. We show that these clusters can be oxidized at electrochemical potentials that are accessible to anoxygenic phototrophs and thus the most likely building blocks for assembly of the first O 2 evolving photoreaction center, most likely originating from green nonsulfur bacteria before the evolution of cyanobacteria.bicarbonate ͉ carbon dioxide ͉ cyanobacteria ͉ evolution ͉ manganese O xygen (O 2 ) production by photosynthesis is by far the dominant global process that replenishes atmospheric and oceanic oxygen essential to sustain all aerobic life. Geochemical records of terrestrial oxides indicate that O 2 evolution must have taken place in the precursors to cyanobacteria before ca. 2.8 billion years ago and led to the accumulation of O 2 in the atmosphere (1, 2). The creation of a photosynthetic apparatus capable of splitting water into O 2 , protons, and electrons was the pivotal innovation in the evolution of life on Earth. For the first time photosynthesis had an unlimited source of electrons and protons by using water as reductant. By freeing photosynthesis from the availability of reduced chemical substances, the global production of organic carbon could be enormously increased and opened new environments for photosynthesis to occur. This event literally changed the face of the Earth. The accumulation of O 2 in the atmosphere led to the biological innovation of aerobic respiration, which harnesses a more powerful metabolic energy source. Because aerobic metabolism generates 18 times more energy (ATP) per metabolic input (hexose sugar) than does anaerobic metabolism, the engine of life became supercharged. This sequence of evolutionary steps enabled the emergence of complex, multicellular, energy-efficient, eukaryotic organisms.Comparisons of cyanobacteria, green algae, ...

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A common ancestor for oxygenic and anoxygenic photosynthetic systems

Cited by 235 publications

References 69 publications

Evidence for two active branches for electron transfer in photosystem I

Evidence for two active branches for electron transfer in photosystem I

Photosynthetic generation of oxygen

The origin of atmospheric oxygen on Earth: The innovation of oxygenic photosynthesis

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