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  • 1
    Electronic Resource
    Electronic Resource
    Spectroscopic studies of the manganese complex of Photosystem II (1993)
    Springer
    Photosynthesis research 38 (1993), S. 341-346 
    Details
    ISSN: 1573-5079
    Keywords: oxygen evolving complex (OEC) ; EPR ; EXAFS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Our recent EPR and EXAFS experiments investigating the structure of the oxygen-evolving complex of PS II are discussed. PS II treatments which affect the cofactors calcium and chloride have been used to poise samples in modified forms of the S-states, S1, S2 and S3. X-ray absorption studies indicate a similar overall structure for the manganese complex between treated and native samples although the influence of the treatments and cofactors is observed. Manganese oxidation (or oxidation of a ligand to the manganese cluster) is indicated to occur on each of the transitions S1 →S2 and S2 →S3 in these modified samples. The cluster appears to contain at least two inequivalent Mn-Mn pairs. In the native samples the Mn-Mn distance is 2.7 Å, but in samples where the calcium site is affected, one of the pairs has a 3.0 Å Mn-Mn distance. The intensity of the 3.3/3.6 Å interaction is reduced on sodium chloride treatment (calcium depletion) perhaps indicating calcium binding close to the manganese cluster. From EPR data we also propose that treatments which affect calcium and chloride binding cause a modification of the native S2 state, slow the reduction of Yz • and allow an S3 EPR signal to be observed following illumination. The origin of the S3 EPR signal, a modified S3 or S2 X• where X• is an organic radical of unknown charge, is discussed in relation to the results from the EXAFS studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00046759
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  • 2
    Electronic Resource
    Electronic Resource
    Patterns of auxin and abscisic acid movement in the tips of gravistimulated primary roots of maize (1996)
    Springer
    Plant growth regulation 20 (1996), S. 253-258 
    Details
    ISSN: 1573-5087
    Keywords: abscisic acid (ABA) ; auxin (IAA) ; gravitropism ; roots ; transport ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Because both abscisic acid (ABA) and auxin (IAA) have been suggested as possible chemical mediators of differential growth during root gravitropism, we compared with redistribution of label from applied 3H-IAA and 3H-ABA during maize root gravitropism and examined the relative basipetal movement of 3H-IAA and 3H-ABA applied to the caps of vertical roots. Lateral movement of 3H-ABA across the tips of vertical roots was non-polar and about 2-fold greater than lateral movement of 3H-IAA (also non-polar). The greater movement of ABA was not due to enhanced uptake since the uptake of 3H-IAA was greater than that of 3H-ABA. Basipetal movement of label from 3H-IAA or 3H-ABA applied to the root cap was determined by measuring radioactivity in successive 1 mm sections behind the tip 90 minutes after application. ABA remained largely in the first mm (point of application) whereas IAA was concentrated in the region 2–4 mm from the tip with substantial levels found 7–8 mm from the tip. Pretreatment with inhibitors of polar auxin transport decreased both gravicurvature and the basipetal movement of IAA. When roots were placed horizontally, the movement of 3H-IAA from top to bottom across the cap was enhanced relative to movement from bottom to top whereas the pattern of movement of label from 3H-ABA was unaffected. These results are consistent with the hypothesis that IAA plays a role in root gravitropism but contrary to the idea that gravi-induced asymmetric distribution of ABA contributes to the response.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00043315
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  • 3
    Electronic Resource
    Electronic Resource
    Calcium-dependent asymmetric movement of 3H-indole-3-acetic acid across gravistimulated isolated root caps of maize (1994)
    Springer
    Plant growth regulation 14 (1994), S. 235-242 
    Details
    ISSN: 1573-5087
    Keywords: auxin transport ; calcium ; gravitropism ; root cap ; Zea mays
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract There is evidence that the cap is the initial site of lateral auxin redistribution during the gravitropic response of roots. We tested this further by comparing asymmetric auxin redistribution across the tips of gravistimulated intact roots, decapped roots, isolated root caps and isolated apical sections taken from decapped roots. Gravistimulation caused asymmetric (downward) auxin movement across the tips of intact roots and isolated root caps but not across the tips of decapped roots or across isolated apical root segments. Naphthylphthalamic acid and pyrenoylbenzoic acid, inhibitors of polar auxin transport, inhibited asymmetric auxin redistribution across gravistimulated isolated root caps and across the tips of gravistimulated intact roots. For intact roots there was a positive correlation between the extent of inhibition of assymmetric auxin redistribution by polar auxin transport inhibitors and the extent of inhibition of asymmetric calcium chelating agent, ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid, also caused parallel inhibition of asymmetric auxin redistribution and gravitropic curvature and this effect was reversed by subsequent treatment with calcium. The results support the hypothesis that the cap is a site of early development of auxin asymmetry in gravistimulated roots and that calcium plays an important role in the development of lateral auxin redistribution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00024798
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  • 4
    Electronic Resource
    Electronic Resource
    Modification of electron transfer from the quinone electron carrier, A1, of Photosystem 1 in a site directed mutant D576→L within the Fe-Sx binding site of PsaA and in second site suppressors of the mutation in Chlamydomonas reinhardtii (1999)
    Springer
    Photosynthesis research 61 (1999), S. 33-42 
    Details
    ISSN: 1573-5079
    Keywords: EPR ; iron-sulphur ; photosynthesis ; P700 ; reaction center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A site directed mutant of the Photosystem I reaction center of Chlamydomonas reinhardtii has been described previously. [Hallahan et al. (1995) Photosynth Res 46: 257–264]. The mutation, PsaA: D576L, changes the conserved aspartate residue adjacent to one of the cysteine ligands binding the Fe-SX center to PsaA. The mutation, which prevents photosynthetic growth, was observed to change the EPR spectrum of the Fe-SA/B centers bound to the PsaC subunit. We suggested that changes in binding of PsaC to the PsaA/PsaB reaction center prevented efficient electron transfer. Second site suppressors of the mutation have now been isolated which have recovered the ability to grow photosynthetically. DNA analysis of four suppressor strains showed the original D576L mutation is intact, and that no mutations are present elsewhere within the Fe-SX binding region of either PsaA or PsaB, nor within PsaC or PsaJ. Subsequent genetic analysis has indicated that the suppressor mutation(s) is nuclear encoded. The suppressors retain the altered binding of PsaC, indicating that this change is not the cause of failure to grow photosynthetically. Further analysis showed that the rate of electron transfer from the quinone electron carrier A1 to Fe-SX is slowed in the mutant (by a factor of approximately two) and restored to wild type rates in the suppressors. ENDOR spectra of A1 ·– in wild-type and mutant preparations are identical, indicating that the electronic structure of the phyllosemiquinone is not changed. The results suggest that the quinone to Fe-SX center electron transfer is sensitive to the structure of the iron-sulfur center, and may be a critical step in the energy conversion process. They also indicate that the structure of the reaction center may be modified as a result of changes in proteins outside the core of the reaction center.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006205811407
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