Three-dimensional structure of system I of photosynthesis at 6 Å resolution

Krauß, Norbert; Hinrichs, Winfried; Witt, I.; Fromme, Petra; Pritzkow, Wolfgang; Dauter, Zbigniew; Betzel, Christian; Wilson, K.S.; Witt, H. T.; Saenger, Wolfram

doi:10.1038/361326a0

Cited by 393 publications

(274 citation statements)

References 43 publications

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“…This subsequent removal of the subunits is in good agreement with proposals for the subunit arrangement by biochemical data [20]. After that, subunit E is located on top of the stromal hump, which was found in the electron density map at 6 8, resolution [14]. Using monomeric PS I complexes the subunits are removed in the same order: first E, after that C and finally D. However the kinetics of the removal is significantly faster.…”

Section: Biochemical Characterization Of the Core Complexessupporting

confidence: 73%

“…Recently the structure of PS I was determined at 6 A resolution [14,15]. In this structure the positions of the three iron sulfur clusters could be unambiguously identified, indicating that Fx has not only an important structural function, but might be directly involved in electron transfer because of the distances between the electron carriers.…”

Section: Introductionmentioning

confidence: 99%

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Spectroscopic characterization of PS I core complexes from thermophilic Synechococcus sp

et al. 1994

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Monomeric and trimeric PS I complexes missing the three stromal subunits E,C and D (termed PS I core complexes) were prepared from the thermophilic cyanobacterium Synechococcus sp. by incubation with urea. The subunits E,C and D are sequentially removed. In the monomeric PS I the subunit C is removed with a half life of approx. 5 min. This is about eight times faster than in the trimeric PS I complex. In parallel with the removal of the FAB containing subunit C the reduction kinetics of P700+ changed from a half life of about 25 ms to about 750 μs. The partner of P700+ in the 750 μs charge recombination was identified to be FX by the difference spectrum of this phase. There are some minor differences in the spectra of trimeric and monomeric PS I core complexes. At 77K the forward electron transfer from A − 1 to FX is blocked in the major fraction of the PS I core complexes and P700+A− 1 recombines with a half life of about 220 μs. In the remaining fraction P700+FX − is formed and decays with a half life of approx. 10 ms at 77 K. The kinetics of the forward electron transfer from A− 1 to the iron‐sulfur‐clusters was measured in the native PS I and the corresponding core complexes. The reoxidation kinetics of A− 1 are identical in both cases (t 12 = 180 ns). We conclude that Fx is an obligatory intermediate in the normal forward electron transfer.

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Section: Biochemical Characterization Of the Core Complexessupporting

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Spectroscopic characterization of PS I core complexes from thermophilic Synechococcus sp

et al. 1994

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“…Furthermore, oligomerization of chlorophyll-&-binding proteins is an essential step in the assembly pathway of the photosynthetic complexes (Hobe et al, 1994;Dreyfuss and Thornber, 1994b;Boekema et al, 1995). In addition to Chls a and b, the different chlorophyllprotein complexes also bind carotenoids (Krauss et al, 1993;Lee and Thornber, 1995), which quench Chl triplet states and thus help prevent the formation of harmful oxygen radicals and singlet oxygen (Siefermann-Harms, 1987). There appears to be an excess of nuclear-encoded and plastid-encoded chlorophyll apoproteins that bind free pigment molecules whenever they are synthesized (Kim et al, 1994).…”

Section: Morphological Cellular and Molecular Events During The Ligmentioning

confidence: 99%

The Regulation of Enzymes Involved in Chlorophyll Biosynthesis

Reinbothe

1996

European Journal of Biochemistry

126

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All living organisms contain tetrapyrroles. In plants, chlorophyll (chlorophyll a plus chlorophyll b) is the most abundant and probably most important tetrapyrrole. It is involved in light absorption and energy transduction during photosynthesis. Chlorophyll is synthesized from the intact carbon skeleton of glutamate via the C, pathway. This pathway takes place in the chloroplast. It is the aim of this review to summarize the current knowledge on the biochemistry and molecular biology of the C,-pathway enzymes, their regulated expression in response to light, and the impact of chlorophyll biosynthesis on chloroplast development. Particular emphasis will be placed on the key regulatory steps of chlorophyll biosynthesis in higher plants, such as 5-aminolevulinic acid formation, the production of Mg*+-protoporphyrin IX, and light-dependent protochlorophyllide reduction.

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“…Nevertheless progress in crystallization of membrane proteins was slow and the 3D structure determinations of membrane proteins are still rare [4][5][6][7][8][9][10][11][12][13]. The numerous difficulties in crystallization of membrane protein have encouraged crystallogenesis studies on this topic, especially on detergents effects.…”

Section: Introductionmentioning

confidence: 99%