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Measurements of mesophyll conductance, photosynthetic electron transport and alternative electron sinks of field grown wheat leaves.

Photosynthesis research

Loreto F, Di Marco G, Tricoli D, Sharkey TD.
PMID: 24310154
Photosynth Res. 1994 Sep;41(3):397-403. doi: 10.1007/BF02183042.

Photosynthetic electron transport drives the carbon reduction cycle, the carbon oxidation cycle, and any alternative electron sinks such as nitrogen reduction. A chlorophyll fluorescence- based method allows estimation of the total electron transport rate while a gas-exchange-based method can...

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Loreto F, Di Marco G, Tricoli D, et al. Measurements of mesophyll conductance, photosynthetic electron transport and alternative electron sinks of field grown wheat leaves. Photosynth Res. 1994;41(3):397-403doi: 10.1007/BF02183042.
Loreto, F., Di Marco, G., Tricoli, D., & Sharkey, T. D. (1994). Measurements of mesophyll conductance, photosynthetic electron transport and alternative electron sinks of field grown wheat leaves. Photosynthesis research, 41(3), 397-403. https://doi.org/10.1007/BF02183042
Loreto, F, et al. "Measurements of mesophyll conductance, photosynthetic electron transport and alternative electron sinks of field grown wheat leaves." Photosynthesis research vol. 41,3 (1994): 397-403. doi: https://doi.org/10.1007/BF02183042
Loreto F, Di Marco G, Tricoli D, Sharkey TD. Measurements of mesophyll conductance, photosynthetic electron transport and alternative electron sinks of field grown wheat leaves. Photosynth Res. 1994 Sep;41(3):397-403. doi: 10.1007/BF02183042. PMID: 24310154.
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Light-emitting diodes as a light source for photosynthesis research.

Photosynthesis research

Tennessen DJ, Singsaas EL, Sharkey TD.
PMID: 24311004
Photosynth Res. 1994 Jan;39(1):85-92. doi: 10.1007/BF00027146.

Light-emitting diodes (LED) can provide large fluxes of red photons and so could be used to make lightweight, efficient lighting systems for photosynthetic research. We compared photosynthesis, stomatal conductance and isoprene emission (a sensitive indicator of ATP status) from...

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Tennessen DJ, Singsaas EL, Sharkey TD. Light-emitting diodes as a light source for photosynthesis research. Photosynth Res. 1994;39(1):85-92doi: 10.1007/BF00027146.
Tennessen, D. J., Singsaas, E. L., & Sharkey, T. D. (1994). Light-emitting diodes as a light source for photosynthesis research. Photosynthesis research, 39(1), 85-92. https://doi.org/10.1007/BF00027146
Tennessen, D J, et al. "Light-emitting diodes as a light source for photosynthesis research." Photosynthesis research vol. 39,1 (1994): 85-92. doi: https://doi.org/10.1007/BF00027146
Tennessen DJ, Singsaas EL, Sharkey TD. Light-emitting diodes as a light source for photosynthesis research. Photosynth Res. 1994 Jan;39(1):85-92. doi: 10.1007/BF00027146. PMID: 24311004.
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Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein.

Photosynthesis research

Sayre RT, Wrobel-Boerner EA.
PMID: 24311210
Photosynth Res. 1994 Apr;40(1):11-9. doi: 10.1007/BF00019041.

We have used antibodies generated against synthetic peptides to determine the topology of the 43 kD chlorophyll a binding protein (CP 43) of Photosystem II. Based on the pattern of proteolytic fragments detected (on western blots) by peptide specific...

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Sayre RT, Wrobel-Boerner EA. Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein. Photosynth Res. 1994;40(1):11-9doi: 10.1007/BF00019041.
Sayre, R. T., & Wrobel-Boerner, E. A. (1994). Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein. Photosynthesis research, 40(1), 11-9. https://doi.org/10.1007/BF00019041
Sayre, R T, and Wrobel-Boerner, E A. "Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein." Photosynthesis research vol. 40,1 (1994): 11-9. doi: https://doi.org/10.1007/BF00019041
Sayre RT, Wrobel-Boerner EA. Molecular topology of the Photosystem II chlorophyll a binding protein, CP 43: Topology of a thylakoid membrane protein. Photosynth Res. 1994 Apr;40(1):11-9. doi: 10.1007/BF00019041. PMID: 24311210.
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Resolution of low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at 77 and 295 K through fluorescence excitation anisotropy.

Photosynthesis research

Woolf VM, Wittmershaus BP, Vermaas WF, Tran TD.
PMID: 24311211
Photosynth Res. 1994 Apr;40(1):21-34. doi: 10.1007/BF00019042.

Fluorescence excitation spectra of highly anisotropic emission from Photosystem I (PS I) were measured at 295 and 77 K on a PS II-less mutant of the cyanobacterium Synechocystis sp. PCC 6803 (S. 6803). When PS I was excited with...

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Woolf VM, Wittmershaus BP, Vermaas WF, et al. Resolution of low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at 77 and 295 K through fluorescence excitation anisotropy. Photosynth Res. 1994;40(1):21-34doi: 10.1007/BF00019042.
Woolf, V. M., Wittmershaus, B. P., Vermaas, W. F., & Tran, T. D. (1994). Resolution of low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at 77 and 295 K through fluorescence excitation anisotropy. Photosynthesis research, 40(1), 21-34. https://doi.org/10.1007/BF00019042
Woolf, V M, et al. "Resolution of low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at 77 and 295 K through fluorescence excitation anisotropy." Photosynthesis research vol. 40,1 (1994): 21-34. doi: https://doi.org/10.1007/BF00019042
Woolf VM, Wittmershaus BP, Vermaas WF, Tran TD. Resolution of low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at 77 and 295 K through fluorescence excitation anisotropy. Photosynth Res. 1994 Apr;40(1):21-34. doi: 10.1007/BF00019042. PMID: 24311211.
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Bill Arnold and calorimetric measurements of the quantum requirement of photosynthesis-once again ahead of his time.

Photosynthesis research

Malkin S, Fork DC.
PMID: 24271284
Photosynth Res. 1996 May;48(1):41-6. doi: 10.1007/BF00040994.

The approach of photocalorimetry to decide on the true quantum requirement of photosynthesis - one of the main issues of the research in the first half of the century and a source of a bitter debate - is described....

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Malkin S, Fork DC. Bill Arnold and calorimetric measurements of the quantum requirement of photosynthesis-once again ahead of his time. Photosynth Res. 1996;48(1):41-6doi: 10.1007/BF00040994.
Malkin, S., & Fork, D. C. (1996). Bill Arnold and calorimetric measurements of the quantum requirement of photosynthesis-once again ahead of his time. Photosynthesis research, 48(1), 41-6. https://doi.org/10.1007/BF00040994
Malkin, S, and Fork, D C. "Bill Arnold and calorimetric measurements of the quantum requirement of photosynthesis-once again ahead of his time." Photosynthesis research vol. 48,1 (1996): 41-6. doi: https://doi.org/10.1007/BF00040994
Malkin S, Fork DC. Bill Arnold and calorimetric measurements of the quantum requirement of photosynthesis-once again ahead of his time. Photosynth Res. 1996 May;48(1):41-6. doi: 10.1007/BF00040994. PMID: 24271284.
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Excitation energy transfer and charge separation in the isolated Photosystem II reaction center.

Photosynthesis research

Greenfield SR, Wasielewski MR.
PMID: 24271289
Photosynth Res. 1996 May;48(1):83-97. doi: 10.1007/BF00040999.

The nature of excitation energy transfer and charge separation in isolated Photosystem II reaction centers is an area of considerable interest and controversy. Excitation energy transfer from accessory chlorophyll a to the primary electron donor P680 takes place in...

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Greenfield SR, Wasielewski MR. Excitation energy transfer and charge separation in the isolated Photosystem II reaction center. Photosynth Res. 1996;48(1):83-97doi: 10.1007/BF00040999.
Greenfield, S. R., & Wasielewski, M. R. (1996). Excitation energy transfer and charge separation in the isolated Photosystem II reaction center. Photosynthesis research, 48(1), 83-97. https://doi.org/10.1007/BF00040999
Greenfield, S R, and Wasielewski, M R. "Excitation energy transfer and charge separation in the isolated Photosystem II reaction center." Photosynthesis research vol. 48,1 (1996): 83-97. doi: https://doi.org/10.1007/BF00040999
Greenfield SR, Wasielewski MR. Excitation energy transfer and charge separation in the isolated Photosystem II reaction center. Photosynth Res. 1996 May;48(1):83-97. doi: 10.1007/BF00040999. PMID: 24271289.
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Thermoluminescence investigations on the site of action of o-phthalaldehyde in photosynthetic electron transport.

Photosynthesis research

Desai TS, Bhagwat AS, Mohanty P.
PMID: 24271301
Photosynth Res. 1996 May;48(1):213-20. doi: 10.1007/BF00041011.

Glow curves from spinach leaf discs infiltrated with o-phthalaldehyde (OPA) show significant similarity to those obtained by DCMU treatment which is known to block the electron flow from QA, the stable acceptor of Photosystem II (PS II). In both...

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Desai TS, Bhagwat AS, Mohanty P. Thermoluminescence investigations on the site of action of o-phthalaldehyde in photosynthetic electron transport. Photosynth Res. 1996;48(1):213-20doi: 10.1007/BF00041011.
Desai, T. S., Bhagwat, A. S., & Mohanty, P. (1996). Thermoluminescence investigations on the site of action of o-phthalaldehyde in photosynthetic electron transport. Photosynthesis research, 48(1), 213-20. https://doi.org/10.1007/BF00041011
Desai, T S, et al. "Thermoluminescence investigations on the site of action of o-phthalaldehyde in photosynthetic electron transport." Photosynthesis research vol. 48,1 (1996): 213-20. doi: https://doi.org/10.1007/BF00041011
Desai TS, Bhagwat AS, Mohanty P. Thermoluminescence investigations on the site of action of o-phthalaldehyde in photosynthetic electron transport. Photosynth Res. 1996 May;48(1):213-20. doi: 10.1007/BF00041011. PMID: 24271301.
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EPR and ENDOR studies of the water oxidizing complex of Photosystem II.

Photosynthesis research

Fiege R, Zweygart W, Bittl R, Adir N, Renger G, Lubitz W.
PMID: 24271303
Photosynth Res. 1996 May;48(1):227-37. doi: 10.1007/BF00041013.

A comparative study of X-band EPR and ENDOR of the S2 state of photosystem II membrane fragments and core complexes in the frozen state is presented. The S2 state was generated either by continuous illumination at T=200 K or...

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Fiege R, Zweygart W, Bittl R, et al. EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynth Res. 1996;48(1):227-37doi: 10.1007/BF00041013.
Fiege, R., Zweygart, W., Bittl, R., Adir, N., Renger, G., & Lubitz, W. (1996). EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynthesis research, 48(1), 227-37. https://doi.org/10.1007/BF00041013
Fiege, R, et al. "EPR and ENDOR studies of the water oxidizing complex of Photosystem II." Photosynthesis research vol. 48,1 (1996): 227-37. doi: https://doi.org/10.1007/BF00041013
Fiege R, Zweygart W, Bittl R, Adir N, Renger G, Lubitz W. EPR and ENDOR studies of the water oxidizing complex of Photosystem II. Photosynth Res. 1996 May;48(1):227-37. doi: 10.1007/BF00041013. PMID: 24271303.
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Competition between annihilation and trapping leads to strongly reduced yields of photochemistry under ps-flash excitation.

Photosynthesis research

Wulf K, Trissl HW.
PMID: 24271306
Photosynth Res. 1996 May;48(1):255-62. doi: 10.1007/BF00041016.

Excitation of photosynthetic systems with short intense flashes is known to lead to exciton-exciton annihilation processes. Here we quantify the effect of competition between annihilation and trapping for Photosystem II, Photosystem I (thylakoids from peas and membranes from the...

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Wulf K, Trissl HW. Competition between annihilation and trapping leads to strongly reduced yields of photochemistry under ps-flash excitation. Photosynth Res. 1996;48(1):255-62doi: 10.1007/BF00041016.
Wulf, K., & Trissl, H. W. (1996). Competition between annihilation and trapping leads to strongly reduced yields of photochemistry under ps-flash excitation. Photosynthesis research, 48(1), 255-62. https://doi.org/10.1007/BF00041016
Wulf, K, and Trissl, H W. "Competition between annihilation and trapping leads to strongly reduced yields of photochemistry under ps-flash excitation." Photosynthesis research vol. 48,1 (1996): 255-62. doi: https://doi.org/10.1007/BF00041016
Wulf K, Trissl HW. Competition between annihilation and trapping leads to strongly reduced yields of photochemistry under ps-flash excitation. Photosynth Res. 1996 May;48(1):255-62. doi: 10.1007/BF00041016. PMID: 24271306.
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Ecophysiological studies in Kalanchoë porphyrocalyx (Baker) and K. miniata (Hils et Bojer), two species performing highly flexible CAM.

Photosynthesis research

Brulfert J, Ravelomanana D, Güçlü S, Kluge M.
PMID: 24271531
Photosynth Res. 1996 Jul;49(1):29-36. doi: 10.1007/BF00029425.

Preceding results, based on the determination of stable carbon isotope composition (δ13C) of leaf tissues from various Kalanchoë species, suggested a close coincidence between the photosynthetic flexibility of the species and their habitat, life form and taxonomic position within...

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Brulfert J, Ravelomanana D, Güçlü S, et al. Ecophysiological studies in Kalanchoë porphyrocalyx (Baker) and K. miniata (Hils et Bojer), two species performing highly flexible CAM. Photosynth Res. 1996;49(1):29-36doi: 10.1007/BF00029425.
Brulfert, J., Ravelomanana, D., Güçlü, S., & Kluge, M. (1996). Ecophysiological studies in Kalanchoë porphyrocalyx (Baker) and K. miniata (Hils et Bojer), two species performing highly flexible CAM. Photosynthesis research, 49(1), 29-36. https://doi.org/10.1007/BF00029425
Brulfert, J, et al. "Ecophysiological studies in Kalanchoë porphyrocalyx (Baker) and K. miniata (Hils et Bojer), two species performing highly flexible CAM." Photosynthesis research vol. 49,1 (1996): 29-36. doi: https://doi.org/10.1007/BF00029425
Brulfert J, Ravelomanana D, Güçlü S, Kluge M. Ecophysiological studies in Kalanchoë porphyrocalyx (Baker) and K. miniata (Hils et Bojer), two species performing highly flexible CAM. Photosynth Res. 1996 Jul;49(1):29-36. doi: 10.1007/BF00029425. PMID: 24271531.
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Supramolecular architecture of cyanobacterial thylakoid membranes: How is the phycobilisome connected with the photosystems?.

Photosynthesis research

Bald D, Kruip J, Rögner M.
PMID: 24271608
Photosynth Res. 1996 Aug;49(2):103-18. doi: 10.1007/BF00117661.

Cyanobacteria, as the most simple organisms to perform oxygenic photosynthesis differ from higher plants especially with respect to the thylakoid membrane structure and the antenna system used to capture light energy. Cyanobacterial antenna systems, the phycobilisomes (PBS), have been...

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Bald D, Kruip J, Rögner M. Supramolecular architecture of cyanobacterial thylakoid membranes: How is the phycobilisome connected with the photosystems?. Photosynth Res. 1996;49(2):103-18doi: 10.1007/BF00117661.
Bald, D., Kruip, J., & Rögner, M. (1996). Supramolecular architecture of cyanobacterial thylakoid membranes: How is the phycobilisome connected with the photosystems?. Photosynthesis research, 49(2), 103-18. https://doi.org/10.1007/BF00117661
Bald, D, et al. "Supramolecular architecture of cyanobacterial thylakoid membranes: How is the phycobilisome connected with the photosystems?." Photosynthesis research vol. 49,2 (1996): 103-18. doi: https://doi.org/10.1007/BF00117661
Bald D, Kruip J, Rögner M. Supramolecular architecture of cyanobacterial thylakoid membranes: How is the phycobilisome connected with the photosystems?. Photosynth Res. 1996 Aug;49(2):103-18. doi: 10.1007/BF00117661. PMID: 24271608.
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15-Cis-β-carotene found in the reaction center of spinach Photosystem I.

Photosynthesis research

Bialek-Bylka GE, Hiyama T, Yumoto K, Koyama Y.
PMID: 24271702
Photosynth Res. 1996 Sep;49(3):245-50. doi: 10.1007/BF00034785.

β-Carotene was extracted from spinach Photosystem I reaction centers (one consisting of the Psa A, B, C, D and E subunits and the other consisting of the Psa A and B subunits alone), and the extract was subjected to...

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Bialek-Bylka GE, Hiyama T, Yumoto K, et al. 15-Cis-β-carotene found in the reaction center of spinach Photosystem I. Photosynth Res. 1996;49(3):245-50doi: 10.1007/BF00034785.
Bialek-Bylka, G. E., Hiyama, T., Yumoto, K., & Koyama, Y. (1996). 15-Cis-β-carotene found in the reaction center of spinach Photosystem I. Photosynthesis research, 49(3), 245-50. https://doi.org/10.1007/BF00034785
Bialek-Bylka, G E, et al. "15-Cis-β-carotene found in the reaction center of spinach Photosystem I." Photosynthesis research vol. 49,3 (1996): 245-50. doi: https://doi.org/10.1007/BF00034785
Bialek-Bylka GE, Hiyama T, Yumoto K, Koyama Y. 15-Cis-β-carotene found in the reaction center of spinach Photosystem I. Photosynth Res. 1996 Sep;49(3):245-50. doi: 10.1007/BF00034785. PMID: 24271702.
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Showing 1 to 12 of 2053 entries