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In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators.

Journal of bioscience and bioengineering

Schnackenberg J, Miyake M, Miyake J, Zorin NA, Asada Y.
PMID: 16232569
J Biosci Bioeng. 1999;88(1):30-4. doi: 10.1016/s1389-1723(99)80171-6.

H2 activation by the oxygen-tolerant hydrogenase from the purple sulfur bacterium Thiocapsa roseopersicina, using electron mediators of cyanobacterial and algal origin, has been demonstrated. Ferredoxins, either from the cyanobacterium Synechococcus PCC7942 or the green alga Scenedesmus obliquus, are capable...

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Schnackenberg J, Miyake M, Miyake J, et al. In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators. J Biosci Bioeng. 1999;88(1):30-4doi: 10.1016/s1389-1723(99)80171-6.
Schnackenberg, J., Miyake, M., Miyake, J., Zorin, N. A., & Asada, Y. (1999). In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators. Journal of bioscience and bioengineering, 88(1), 30-4. https://doi.org/10.1016/s1389-1723(99)80171-6
Schnackenberg, J, et al. "In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators." Journal of bioscience and bioengineering vol. 88,1 (1999): 30-4. doi: https://doi.org/10.1016/s1389-1723(99)80171-6
Schnackenberg J, Miyake M, Miyake J, Zorin NA, Asada Y. In vitro and in vivo coupling of Thiocapsa hydrogenase with cyanobacterial and algal electron mediators. J Biosci Bioeng. 1999;88(1):30-4. doi: 10.1016/s1389-1723(99)80171-6. PMID: 16232569.
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Mossbauer spectroscopic study of functional thermal destruction of iron--sulfur proteins in membranes of thermophilic cyanobacteria synechococcus elongatus .

Biochemistry. Biokhimiia

Aleksandrov AY, Belevich NP, Davletshina LN, Ivanov II, Kaurov YN, Khval'kovskaya EA, Novakova AA, Rubin AB, Semin BK.
PMID: 10187909
Biochemistry (Mosc). 1999 Feb;64(2):181-8.

A mathematical model of the Mossbauer spectrum (80K) of native membranes of Synechococcus elongatus was constructed on the basis of values of the quadruple splitting (Delta) and the isomeric shift (delta) of the iron-containing components of the photosynthetic apparatus...

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Aleksandrov AY, Belevich NP, Davletshina LN, et al. Mossbauer spectroscopic study of functional thermal destruction of iron--sulfur proteins in membranes of thermophilic cyanobacteria synechococcus elongatus . Biochemistry (Mosc). 1999;64(2):181-8
Aleksandrov, A. Y., Belevich, N. P., Davletshina, L. N., Ivanov, I. I., Kaurov, Y. N., Khval'kovskaya, E. A., Novakova, A. A., Rubin, A. B., & Semin, B. K. (1999). Mossbauer spectroscopic study of functional thermal destruction of iron--sulfur proteins in membranes of thermophilic cyanobacteria synechococcus elongatus . Biochemistry. Biokhimiia, 64(2), 181-8.
Aleksandrov, et al. "Mossbauer spectroscopic study of functional thermal destruction of iron--sulfur proteins in membranes of thermophilic cyanobacteria synechococcus elongatus ." Biochemistry. Biokhimiia vol. 64,2 (1999): 181-8.
Aleksandrov AY, Belevich NP, Davletshina LN, Ivanov II, Kaurov YN, Khval'kovskaya EA, Novakova AA, Rubin AB, Semin BK. Mossbauer spectroscopic study of functional thermal destruction of iron--sulfur proteins in membranes of thermophilic cyanobacteria synechococcus elongatus . Biochemistry (Mosc). 1999 Feb;64(2):181-8. PMID: 10187909.
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Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria.

Photosynthesis research

Matsubara H, Oh-Oka H, Takahashi Y, Fujita Y.
PMID: 24301573
Photosynth Res. 1995 Nov;46(1):107-15. doi: 10.1007/BF00020421.

A brief review is presented on the gene products of frxA, frxB and frxC found in chloroplasts. The product of frxA shows high sequence homologies to bacterial 2[4Fe-4S] ferredoxins, but it functions as iron-sulfur centers A and B in...

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Matsubara H, Oh-Oka H, Takahashi Y, et al. Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria. Photosynth Res. 1995;46(1):107-15doi: 10.1007/BF00020421.
Matsubara, H., Oh-Oka, H., Takahashi, Y., & Fujita, Y. (1995). Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria. Photosynthesis research, 46(1), 107-15. https://doi.org/10.1007/BF00020421
Matsubara, H, et al. "Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria." Photosynthesis research vol. 46,1 (1995): 107-15. doi: https://doi.org/10.1007/BF00020421
Matsubara H, Oh-Oka H, Takahashi Y, Fujita Y. Three iron-sulfur proteins encoded by three ORFs in chloroplasts and cyanobacteria. Photosynth Res. 1995 Nov;46(1):107-15. doi: 10.1007/BF00020421. PMID: 24301573.
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Expression of Anabaena ferredoxin genes in Escherichia coli.

Plant molecular biology

Böhme H, Haselkorn R.
PMID: 24271199
Plant Mol Biol. 1989 Jun;12(6):667-72. doi: 10.1007/BF00044157.

The genes for ferredoxin from heterocysts (fdx H) and vegetative cells (pet F) of Anabaena sp. strain 7120 were subcloned into plasmid pUC 18/19. Both genes were expressed in Escherichia coli at high levels (≈10% of total protein). Pet...

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Böhme H, Haselkorn R. Expression of Anabaena ferredoxin genes in Escherichia coli. Plant Mol Biol. 1989;12(6):667-72doi: 10.1007/BF00044157.
Böhme, H., & Haselkorn, R. (1989). Expression of Anabaena ferredoxin genes in Escherichia coli. Plant molecular biology, 12(6), 667-72. https://doi.org/10.1007/BF00044157
Böhme, H, and Haselkorn, R. "Expression of Anabaena ferredoxin genes in Escherichia coli." Plant molecular biology vol. 12,6 (1989): 667-72. doi: https://doi.org/10.1007/BF00044157
Böhme H, Haselkorn R. Expression of Anabaena ferredoxin genes in Escherichia coli. Plant Mol Biol. 1989 Jun;12(6):667-72. doi: 10.1007/BF00044157. PMID: 24271199.
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Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen fixation and photosynthesis in Anabaena sp.

Photosynthesis research

Razquin P, Schmitz S, Peleato ML, Fillat MF, Gómez-Moreno C, Böhme H.
PMID: 24306637
Photosynth Res. 1995 Jan;43(1):35-40. doi: 10.1007/BF00029460.

In cyanobacteria an increasing number of low potential electron carriers is found, but in most cases their contribution to metabolic pathways remains unclear. In this work, we compare recombinant plant-type ferredoxins from Anabaena sp. PCC 7120, encoded by the...

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Razquin P, Schmitz S, Peleato ML, et al. Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen fixation and photosynthesis in Anabaena sp. Photosynth Res. 1995;43(1):35-40doi: 10.1007/BF00029460.
Razquin, P., Schmitz, S., Peleato, M. L., Fillat, M. F., Gómez-Moreno, C., & Böhme, H. (1995). Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen fixation and photosynthesis in Anabaena sp. Photosynthesis research, 43(1), 35-40. https://doi.org/10.1007/BF00029460
Razquin, P, et al. "Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen fixation and photosynthesis in Anabaena sp." Photosynthesis research vol. 43,1 (1995): 35-40. doi: https://doi.org/10.1007/BF00029460
Razquin P, Schmitz S, Peleato ML, Fillat MF, Gómez-Moreno C, Böhme H. Differential activities of heterocyst ferredoxin, vegetative cell ferredoxin, and flavodoxin as electron carriers in nitrogen fixation and photosynthesis in Anabaena sp. Photosynth Res. 1995 Jan;43(1):35-40. doi: 10.1007/BF00029460. PMID: 24306637.
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Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.).

Photosynthesis research

Kamide K, Sakai H, Aoki K, Sanada Y, Wada K, Green LS, Yee BC, Buchanan BB.
PMID: 24301596
Photosynth Res. 1995 Nov;46(1):301-8. doi: 10.1007/BF00020444.

Several forms (isoproteins) of ferredoxin in roots, leaves, and green and red pericarps in tomato plants (Lycopersicon esculentum Mill.) were earlier identified on the basis of N-terminal amino acid sequence and chromatographic behavior (Green et al. 1991). In the...

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Kamide K, Sakai H, Aoki K, et al. Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.). Photosynth Res. 1995;46(1):301-8doi: 10.1007/BF00020444.
Kamide, K., Sakai, H., Aoki, K., Sanada, Y., Wada, K., Green, L. S., Yee, B. C., & Buchanan, B. B. (1995). Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.). Photosynthesis research, 46(1), 301-8. https://doi.org/10.1007/BF00020444
Kamide, K, et al. "Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.)." Photosynthesis research vol. 46,1 (1995): 301-8. doi: https://doi.org/10.1007/BF00020444
Kamide K, Sakai H, Aoki K, Sanada Y, Wada K, Green LS, Yee BC, Buchanan BB. Amino acid sequences of heterotrophic and photosynthetic ferredoxins from the tomato plant (Lycopersicon esculentum Mill.). Photosynth Res. 1995 Nov;46(1):301-8. doi: 10.1007/BF00020444. PMID: 24301596.
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FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors.

Frontiers in plant science

Guan X, Chen S, Voon CP, Wong KB, Tikkanen M, Lim BL.
PMID: 29670639
Front Plant Sci. 2018 Apr 04;9:410. doi: 10.3389/fpls.2018.00410. eCollection 2018.

Plant-type ferredoxins in Arabidopsis transfer electrons from the photosystem I to multiple redox-driven enzymes involved in the assimilation of carbon, nitrogen, and sulfur. Leaf-type ferredoxins also modulate the switch between the linear and cyclic electron routes of the photosystems....

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Guan X, Chen S, Voon CP, et al. FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors. Front Plant Sci. 2018;9:410doi: 10.3389/fpls.2018.00410.
Guan, X., Chen, S., Voon, C. P., Wong, K. B., Tikkanen, M., & Lim, B. L. (2018). FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors. Frontiers in plant science, 9410. https://doi.org/10.3389/fpls.2018.00410
Guan, Xiaoqian, et al. "FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors." Frontiers in plant science vol. 9 (2018): 410. doi: https://doi.org/10.3389/fpls.2018.00410
Guan X, Chen S, Voon CP, Wong KB, Tikkanen M, Lim BL. FdC1 and Leaf-Type Ferredoxins Channel Electrons From Photosystem I to Different Downstream Electron Acceptors. Front Plant Sci. 2018 Apr 04;9:410. doi: 10.3389/fpls.2018.00410. eCollection 2018. PMID: 29670639; PMCID: PMC5893904.
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An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions.

Biophysical reviews

Chiliza ZE, Martínez-Oyanedel J, Syed K.
PMID: 32885385
Biophys Rev. 2020 Oct;12(5):1217-1222. doi: 10.1007/s12551-020-00749-7. Epub 2020 Sep 03.

Cytochrome P450 monooxygenases (CYPs/P450s) are heme-thiolate proteins that are ubiquitously present in organisms, including non-living entities such as viruses. With the exception of self-sufficient P450s, all other P450 enzymes need electrons to perform their enzymatic activity and these electrons...

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Chiliza ZE, Martínez-Oyanedel J, Syed K. An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions. Biophys Rev. 2020;12(5):1217-1222doi: 10.1007/s12551-020-00749-7.
Chiliza, Z. E., Martínez-Oyanedel, J., & Syed, K. (2020). An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions. Biophysical reviews, 12(5), 1217-1222. https://doi.org/10.1007/s12551-020-00749-7
Chiliza, Zinhle Edith, et al. "An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions." Biophysical reviews vol. 12,5 (2020): 1217-1222. doi: https://doi.org/10.1007/s12551-020-00749-7
Chiliza ZE, Martínez-Oyanedel J, Syed K. An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions. Biophys Rev. 2020 Oct;12(5):1217-1222. doi: 10.1007/s12551-020-00749-7. Epub 2020 Sep 03. PMID: 32885385; PMCID: PMC7575658.
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Further characterization of Nostoc verrucosum ferredoxins.

Plant & cell physiology

Shin M, Yokoyama Z, Oshino R, Sukenobu M, Kitazume Y.
PMID: 25385986
Plant Cell Physiol. 1980 Dec;21(8):1681-4. doi: 10.1093/pcp/21.8.1681.

Nostoc verrucosum ferredoxins Fd I and Fd II were found to have different amino acid compositions. Fd I had 98 amino acid residues of Trpo, Lys4, His1, Arg1, Asp14, Thr8, Ser6, Glu14, Pro4, Gly7, Ala10, Cys4, Val5, Met0, Ile6,...

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Shin M, Yokoyama Z, Oshino R, et al. Further characterization of Nostoc verrucosum ferredoxins. Plant Cell Physiol. 1980;21(8):1681-4doi: 10.1093/pcp/21.8.1681.
Shin, M., Yokoyama, Z., Oshino, R., Sukenobu, M., & Kitazume, Y. (1980). Further characterization of Nostoc verrucosum ferredoxins. Plant & cell physiology, 21(8), 1681-4. https://doi.org/10.1093/pcp/21.8.1681
Shin, M, et al. "Further characterization of Nostoc verrucosum ferredoxins." Plant & cell physiology vol. 21,8 (1980): 1681-4. doi: https://doi.org/10.1093/pcp/21.8.1681
Shin M, Yokoyama Z, Oshino R, Sukenobu M, Kitazume Y. Further characterization of Nostoc verrucosum ferredoxins. Plant Cell Physiol. 1980 Dec;21(8):1681-4. doi: 10.1093/pcp/21.8.1681. PMID: 25385986.
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Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances.

Life (Basel, Switzerland)

Cassier-Chauvat C, Chauvat F.
PMID: 25387163
Life (Basel). 2014 Nov 07;4(4):666-80. doi: 10.3390/life4040666.

Ferredoxins (Fed), occurring in most organisms, are small proteins that use their iron-sulfur cluster to distribute electrons to various metabolic pathways, likely including hydrogen production. Here, we summarize the current knowledge on ferredoxins in cyanobacteria, the prokaryotes regarded as...

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Cassier-Chauvat C, Chauvat F. Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances. Life (Basel). 2014;4(4):666-80doi: 10.3390/life4040666.
Cassier-Chauvat, C., & Chauvat, F. (2014). Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances. Life (Basel, Switzerland), 4(4), 666-80. https://doi.org/10.3390/life4040666
Cassier-Chauvat, Corinne, and Chauvat, Franck. "Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances." Life (Basel, Switzerland) vol. 4,4 (2014): 666-80. doi: https://doi.org/10.3390/life4040666
Cassier-Chauvat C, Chauvat F. Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances. Life (Basel). 2014 Nov 07;4(4):666-80. doi: 10.3390/life4040666. PMID: 25387163; PMCID: PMC4284462.
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Investigation of the Ferredoxin's Influence on the Anaerobic and Aerobic, Enzymatic H.

Frontiers in bioengineering and biotechnology

Koo J, Cha Y.
PMID: 33718343
Front Bioeng Biotechnol. 2021 Feb 26;9:641305. doi: 10.3389/fbioe.2021.641305. eCollection 2021.

Ferredoxins are metalloproteins that deliver electrons to several redox partners, including [FeFe] hydrogenases that are potentially a component of biological H

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Koo J, Cha Y. Investigation of the Ferredoxin's Influence on the Anaerobic and Aerobic, Enzymatic H. Front Bioeng Biotechnol. 2021;9:641305doi: 10.3389/fbioe.2021.641305.
Koo, J., & Cha, Y. (2021). Investigation of the Ferredoxin's Influence on the Anaerobic and Aerobic, Enzymatic H. Frontiers in bioengineering and biotechnology, 9641305. https://doi.org/10.3389/fbioe.2021.641305
Koo, Jamin, and Cha, Yeeun. "Investigation of the Ferredoxin's Influence on the Anaerobic and Aerobic, Enzymatic H." Frontiers in bioengineering and biotechnology vol. 9 (2021): 641305. doi: https://doi.org/10.3389/fbioe.2021.641305
Koo J, Cha Y. Investigation of the Ferredoxin's Influence on the Anaerobic and Aerobic, Enzymatic H. Front Bioeng Biotechnol. 2021 Feb 26;9:641305. doi: 10.3389/fbioe.2021.641305. eCollection 2021. PMID: 33718343; PMCID: PMC7952640.
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Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds.

Inorganic chemistry

Ueyama N, Yamada Y, Okamura Ta, Kimura S, Nakamura A.
PMID: 11666795
Inorg Chem. 1996 Oct 23;35(22):6473-6484. doi: 10.1021/ic9604324.

Iron-sulfur clusters containing a singly or doubly NH.S hydrogen-bonded arenethiolate ligand, [Fe(4)S(4)(S-2-RCONHC(6)H(4))(4)](2)(-) (R = CH(3), t-Bu, CF(3)), [Fe(4)S(4){S-2,6-(RCONH)(2)C(6)H(3)}(4)](2)(-), [Fe(2)S(2)(S-2-RCONHC(6)H(4))(4)](2)(-) (R = CH(3), t-Bu, CF(3)), and [Fe(2)S(2){S-2,6-(RCONH)(2)C(6)H(3)}(4)](2)(-), were synthesized as models of bacterial [4Fe-4S] and plant-type [2Fe-2S] ferredoxins. The X-ray...

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Ueyama N, Yamada Y, Okamura Ta, et al. Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds. Inorg Chem. 1996;35(22):6473-6484doi: 10.1021/ic9604324.
Ueyama, N., Yamada, Y., Okamura Ta, Kimura, S., & Nakamura, A. (1996). Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds. Inorganic chemistry, 35(22), 6473-6484. https://doi.org/10.1021/ic9604324
Ueyama, Norikazu, et al. "Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds." Inorganic chemistry vol. 35,22 (1996): 6473-6484. doi: https://doi.org/10.1021/ic9604324
Ueyama N, Yamada Y, Okamura Ta, Kimura S, Nakamura A. Structure and Properties of [Fe(4)S(4){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-) and [Fe(2)S(2){2,6-bis(acylamino)benzenethiolato-S}(4)](2)(-): Protection of the Fe-S Bond by Double NH.S Hydrogen Bonds. Inorg Chem. 1996 Oct 23;35(22):6473-6484. doi: 10.1021/ic9604324. PMID: 11666795.
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Showing 25 to 36 of 45 entries