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Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster.

Proceedings of the National Academy of Sciences of the United States of America

Job RC, Bruice TC.
PMID: 16592256
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2478-82. doi: 10.1073/pnas.72.7.2478.

The water-soluble tetranuclear iron-sulfur cluster ion Fe(4)S(4)(SCH(2)CH(2)CO(2) (-))(4) (6-) (II) has been prepared. The stability of II in water is sufficient to allow the spectrotitrimetric determination of the pK(a) of its Fe(4)S(4) core as 7.4. In our hands the...

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Job RC, Bruice TC. Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster. Proc Natl Acad Sci U S A. 1975;72(7):2478-82doi: 10.1073/pnas.72.7.2478.
Job, R. C., & Bruice, T. C. (1975). Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster. Proceedings of the National Academy of Sciences of the United States of America, 72(7), 2478-82. https://doi.org/10.1073/pnas.72.7.2478
Job, R C, and Bruice, T C. "Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster." Proceedings of the National Academy of Sciences of the United States of America vol. 72,7 (1975): 2478-82. doi: https://doi.org/10.1073/pnas.72.7.2478
Job RC, Bruice TC. Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2478-82. doi: 10.1073/pnas.72.7.2478. PMID: 16592256; PMCID: PMC432790.
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Isolation and Characterization of a Ferredoxin Gene from Arabidopsis thaliana.

Plant physiology

Somers DE, Caspar T, Quail PH.
PMID: 16667505
Plant Physiol. 1990 Jun;93(2):572-7. doi: 10.1104/pp.93.2.572.

We report the cloning and characterization of an Arabidopsis thaliana (L.) Heynh. (Columbia ecotype) ferredoxin gene (Fed A). Sequence analysis of a genomic clone shows an intron-free, 444-base pair open reading frame which encodes a 96 amino acid mature...

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Somers DE, Caspar T, Quail PH. Isolation and Characterization of a Ferredoxin Gene from Arabidopsis thaliana. Plant Physiol. 1990;93(2):572-7doi: 10.1104/pp.93.2.572.
Somers, D. E., Caspar, T., & Quail, P. H. (1990). Isolation and Characterization of a Ferredoxin Gene from Arabidopsis thaliana. Plant physiology, 93(2), 572-7. https://doi.org/10.1104/pp.93.2.572
Somers, D E, et al. "Isolation and Characterization of a Ferredoxin Gene from Arabidopsis thaliana." Plant physiology vol. 93,2 (1990): 572-7. doi: https://doi.org/10.1104/pp.93.2.572
Somers DE, Caspar T, Quail PH. Isolation and Characterization of a Ferredoxin Gene from Arabidopsis thaliana. Plant Physiol. 1990 Jun;93(2):572-7. doi: 10.1104/pp.93.2.572. PMID: 16667505; PMCID: PMC1062552.
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Revisiting the Electronic Structure of FeS Monomers Using ab Initio Ligand Field Theory and the Angular Overlap Model.

Inorganic chemistry

Chilkuri VG, DeBeer S, Neese F.
PMID: 28829123
Inorg Chem. 2017 Sep 05;56(17):10418-10436. doi: 10.1021/acs.inorgchem.7b01371. Epub 2017 Aug 22.

Iron-sulfur (FeS) proteins are universally found in nature with actives sites ranging in complexity from simple monomers to multinuclear sites from two up to eight iron atoms. These sites include mononuclear (rubredoxins), dinuclear (ferredoxins and Rieske proteins), trinuclear (e.g.,...

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Chilkuri VG, DeBeer S, Neese F. Revisiting the Electronic Structure of FeS Monomers Using ab Initio Ligand Field Theory and the Angular Overlap Model. Inorg Chem. 2017;56(17):10418-10436doi: 10.1021/acs.inorgchem.7b01371.
Chilkuri, V. G., DeBeer, S., & Neese, F. (2017). Revisiting the Electronic Structure of FeS Monomers Using ab Initio Ligand Field Theory and the Angular Overlap Model. Inorganic chemistry, 56(17), 10418-10436. https://doi.org/10.1021/acs.inorgchem.7b01371
Chilkuri, Vijay Gopal, et al. "Revisiting the Electronic Structure of FeS Monomers Using ab Initio Ligand Field Theory and the Angular Overlap Model." Inorganic chemistry vol. 56,17 (2017): 10418-10436. doi: https://doi.org/10.1021/acs.inorgchem.7b01371
Chilkuri VG, DeBeer S, Neese F. Revisiting the Electronic Structure of FeS Monomers Using ab Initio Ligand Field Theory and the Angular Overlap Model. Inorg Chem. 2017 Sep 05;56(17):10418-10436. doi: 10.1021/acs.inorgchem.7b01371. Epub 2017 Aug 22. PMID: 28829123.
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Functional Stability and Community Dynamics during Spring and Autumn Seasons Over 3 Years in Camargue Microbial Mats.

Frontiers in microbiology

Berlanga M, Palau M, Guerrero R.
PMID: 29312277
Front Microbiol. 2017 Dec 22;8:2619. doi: 10.3389/fmicb.2017.02619. eCollection 2017.

Microbial mats are complex biofilms in which the major element cycles are represented at a millimeter scale. In this study, community variability within microbial mats from the Camargue wetlands (Rhone Delta, southern France) were analyzed over 3 years during...

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Berlanga M, Palau M, Guerrero R. Functional Stability and Community Dynamics during Spring and Autumn Seasons Over 3 Years in Camargue Microbial Mats. Front Microbiol. 2017;8:2619doi: 10.3389/fmicb.2017.02619.
Berlanga, M., Palau, M., & Guerrero, R. (2017). Functional Stability and Community Dynamics during Spring and Autumn Seasons Over 3 Years in Camargue Microbial Mats. Frontiers in microbiology, 82619. https://doi.org/10.3389/fmicb.2017.02619
Berlanga, Mercedes, et al. "Functional Stability and Community Dynamics during Spring and Autumn Seasons Over 3 Years in Camargue Microbial Mats." Frontiers in microbiology vol. 8 (2017): 2619. doi: https://doi.org/10.3389/fmicb.2017.02619
Berlanga M, Palau M, Guerrero R. Functional Stability and Community Dynamics during Spring and Autumn Seasons Over 3 Years in Camargue Microbial Mats. Front Microbiol. 2017 Dec 22;8:2619. doi: 10.3389/fmicb.2017.02619. eCollection 2017. PMID: 29312277; PMCID: PMC5744480.
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Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis.

The Plant cell

Stuart D, Sandström M, Youssef HM, Zakhrabekova S, Jensen PE, Bollivar D, Hansson M.
PMID: 34051099
Plant Cell. 2021 Aug 31;33(8):2834-2849. doi: 10.1093/plcell/koab150.

Ferredoxins are single-electron carrier proteins involved in various cellular reactions. In chloroplasts, the most abundant ferredoxin accepts electrons from photosystem I and shuttles electrons via ferredoxin NADP+ oxidoreductase to generate NADPH or directly to ferredoxin dependent enzymes. In addition,...

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Stuart D, Sandström M, Youssef HM, et al. Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. Plant Cell. 2021;33(8):2834-2849doi: 10.1093/plcell/koab150.
Stuart, D., Sandström, M., Youssef, H. M., Zakhrabekova, S., Jensen, P. E., Bollivar, D., & Hansson, M. (2021). Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. The Plant cell, 33(8), 2834-2849. https://doi.org/10.1093/plcell/koab150
Stuart, David, et al. "Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis." The Plant cell vol. 33,8 (2021): 2834-2849. doi: https://doi.org/10.1093/plcell/koab150
Stuart D, Sandström M, Youssef HM, Zakhrabekova S, Jensen PE, Bollivar D, Hansson M. Barley Viridis-k links an evolutionarily conserved C-type ferredoxin to chlorophyll biosynthesis. Plant Cell. 2021 Aug 31;33(8):2834-2849. doi: 10.1093/plcell/koab150. PMID: 34051099; PMCID: PMC8408499.
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Are plastocyanin and ferredoxin specific electron carriers or generic redox capacitors? Classical and murburn perspectives on two photosynthetic proteins.

Journal of biomolecular structure & dynamics

Gideon DA, Nirusimhan V, Manoj KM.
PMID: 33073701
J Biomol Struct Dyn. 2020 Oct 19;1-15. doi: 10.1080/07391102.2020.1835715. Epub 2020 Oct 19.

In the light reaction of oxygenic photosynthesis, plastocyanin (PC) and ferredoxins (Fd) are small/diffusible redox-active proteins playing key roles in electron transfer/transport phenomena. In the Z-scheme mechanistic purview, they are considered as specific affinity binding-based electron-relay agents, linking the...

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Gideon DA, Nirusimhan V, Manoj KM. Are plastocyanin and ferredoxin specific electron carriers or generic redox capacitors? Classical and murburn perspectives on two photosynthetic proteins. J Biomol Struct Dyn. 2020;1-15doi: 10.1080/07391102.2020.1835715.
Gideon, D. A., Nirusimhan, V., & Manoj, K. M. (2020). Are plastocyanin and ferredoxin specific electron carriers or generic redox capacitors? Classical and murburn perspectives on two photosynthetic proteins. Journal of biomolecular structure & dynamics, 1-15. https://doi.org/10.1080/07391102.2020.1835715
Gideon, Daniel Andrew, et al. "Are plastocyanin and ferredoxin specific electron carriers or generic redox capacitors? Classical and murburn perspectives on two photosynthetic proteins." Journal of biomolecular structure & dynamics vol. (2020): 1-15. doi: https://doi.org/10.1080/07391102.2020.1835715
Gideon DA, Nirusimhan V, Manoj KM. Are plastocyanin and ferredoxin specific electron carriers or generic redox capacitors? Classical and murburn perspectives on two photosynthetic proteins. J Biomol Struct Dyn. 2020 Oct 19;1-15. doi: 10.1080/07391102.2020.1835715. Epub 2020 Oct 19. PMID: 33073701.
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The ferredoxin-encoding fdxN gene of the filamentous cyanobacterium Anabaena variabilis ATCC 29413 is not essential for nitrogen fixation.

The New phytologist

Masepohl B, Görlitz K, Monnerjahn U, Moslerand B, Böhme H.
PMID: 33863005
New Phytol. 1997 Jul;136(3):419-423. doi: 10.1046/j.1469-8137.1997.00771.x.

In contrast to that of Anabaena sp. PCC7120, the fdxN gene in Anabaena variabilis ATCC 29413 is not interrupted by a 55-kb DNA element, making this strain more suitable for genetic analysis of fdxN independent of the developmentally regulated...

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Masepohl B, Görlitz K, Monnerjahn U, et al. The ferredoxin-encoding fdxN gene of the filamentous cyanobacterium Anabaena variabilis ATCC 29413 is not essential for nitrogen fixation. New Phytol. 1997;136(3):419-423doi: 10.1046/j.1469-8137.1997.00771.x.
Masepohl, B., Görlitz, K., Monnerjahn, U., Moslerand, B., & Böhme, H. (1997). The ferredoxin-encoding fdxN gene of the filamentous cyanobacterium Anabaena variabilis ATCC 29413 is not essential for nitrogen fixation. The New phytologist, 136(3), 419-423. https://doi.org/10.1046/j.1469-8137.1997.00771.x
Masepohl, Bernd, et al. "The ferredoxin-encoding fdxN gene of the filamentous cyanobacterium Anabaena variabilis ATCC 29413 is not essential for nitrogen fixation." The New phytologist vol. 136,3 (1997): 419-423. doi: https://doi.org/10.1046/j.1469-8137.1997.00771.x
Masepohl B, Görlitz K, Monnerjahn U, Moslerand B, Böhme H. The ferredoxin-encoding fdxN gene of the filamentous cyanobacterium Anabaena variabilis ATCC 29413 is not essential for nitrogen fixation. New Phytol. 1997 Jul;136(3):419-423. doi: 10.1046/j.1469-8137.1997.00771.x. PMID: 33863005.
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Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites.

Proceedings of the National Academy of Sciences of the United States of America

Rawlings J, Siiman O, Gray HB.
PMID: 16592130
Proc Natl Acad Sci U S A. 1974 Jan;71(1):125-7. doi: 10.1073/pnas.71.1.125.

The electronic absorption spectra of oxidized and reduced spinach ferredoxins have been measured between 1200 and 600 nm at low temperature in D(2)O/ethylene glycol glasses. Relatively weak absorption bands are observed at 720, 820, and 920 nm in oxidized...

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Rawlings J, Siiman O, Gray HB. Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proc Natl Acad Sci U S A. 1974;71(1):125-7doi: 10.1073/pnas.71.1.125.
Rawlings, J., Siiman, O., & Gray, H. B. (1974). Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proceedings of the National Academy of Sciences of the United States of America, 71(1), 125-7. https://doi.org/10.1073/pnas.71.1.125
Rawlings, J, et al. "Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites." Proceedings of the National Academy of Sciences of the United States of America vol. 71,1 (1974): 125-7. doi: https://doi.org/10.1073/pnas.71.1.125
Rawlings J, Siiman O, Gray HB. Low Temperature Electronic Absorption Spectra of Oxidized and Reduced Spinach Ferredoxins. Evidence for Nonequivalent Iron(III) Sites. Proc Natl Acad Sci U S A. 1974 Jan;71(1):125-7. doi: 10.1073/pnas.71.1.125. PMID: 16592130; PMCID: PMC387948.
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Creation and ESR identification, in single crystals, of synthetic analogs of the S=(1/2) states of the Fe4S4 cores of the reduced ferredoxins and oxidized high-potential proteins.

Physical review letters

Gloux J, Gloux P, Lamotte B, Rius aG.
PMID: 10031562
Phys Rev Lett. 1985 Feb 11;54(6):599-602. doi: 10.1103/PhysRevLett.54.599.

No abstract available.

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Gloux J, Gloux P, Lamotte B, et al. Creation and ESR identification, in single crystals, of synthetic analogs of the S=(1/2) states of the Fe4S4 cores of the reduced ferredoxins and oxidized high-potential proteins. Phys Rev Lett. 1985;54(6):599-602doi: 10.1103/PhysRevLett.54.599.
Gloux, J., Gloux, P., Lamotte, B., & Rius, a. G. (1985). Creation and ESR identification, in single crystals, of synthetic analogs of the S=(1/2) states of the Fe4S4 cores of the reduced ferredoxins and oxidized high-potential proteins. Physical review letters, 54(6), 599-602. https://doi.org/10.1103/PhysRevLett.54.599
Gloux, et al. "Creation and ESR identification, in single crystals, of synthetic analogs of the S=(1/2) states of the Fe4S4 cores of the reduced ferredoxins and oxidized high-potential proteins." Physical review letters vol. 54,6 (1985): 599-602. doi: https://doi.org/10.1103/PhysRevLett.54.599
Gloux J, Gloux P, Lamotte B, Rius aG. Creation and ESR identification, in single crystals, of synthetic analogs of the S=(1/2) states of the Fe4S4 cores of the reduced ferredoxins and oxidized high-potential proteins. Phys Rev Lett. 1985 Feb 11;54(6):599-602. doi: 10.1103/PhysRevLett.54.599. PMID: 10031562.
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Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA.

Plant molecular biology

Dunn PP, Gray JC.
PMID: 24272344
Plant Mol Biol. 1988 May;11(3):311-9. doi: 10.1007/BF00027388.

The gene for the 8 kDa subunit of photosystem I has been located in the small single copy region of wheat chloroplast DNA by coupled transcription-translation of cloned fragments of DNA and by DNA sequence analysis. The pea gene...

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Dunn PP, Gray JC. Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. Plant Mol Biol. 1988;11(3):311-9doi: 10.1007/BF00027388.
Dunn, P. P., & Gray, J. C. (1988). Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. Plant molecular biology, 11(3), 311-9. https://doi.org/10.1007/BF00027388
Dunn, P P, and Gray, J C. "Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA." Plant molecular biology vol. 11,3 (1988): 311-9. doi: https://doi.org/10.1007/BF00027388
Dunn PP, Gray JC. Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. Plant Mol Biol. 1988 May;11(3):311-9. doi: 10.1007/BF00027388. PMID: 24272344.
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Diversification of Ferredoxins across Living Organisms.

Current issues in molecular biology

Nzuza N, Padayachee T, Chen W, Gront D, Nelson DR, Syed K.
PMID: 34698119
Curr Issues Mol Biol. 2021 Sep 30;43(3):1374-1390. doi: 10.3390/cimb43030098.

Ferredoxins, iron-sulfur (Fe-S) cluster proteins, play a key role in oxidoreduction reactions. To date, evolutionary analysis of these proteins across the domains of life have been confined to observing the abundance of Fe-S cluster types (2Fe-2S, 3Fe-4S, 4Fe-4S, 7Fe-8S...

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Nzuza N, Padayachee T, Chen W, et al. Diversification of Ferredoxins across Living Organisms. Curr Issues Mol Biol. 2021;43(3):1374-1390doi: 10.3390/cimb43030098.
Nzuza, N., Padayachee, T., Chen, W., Gront, D., Nelson, D. R., & Syed, K. (2021). Diversification of Ferredoxins across Living Organisms. Current issues in molecular biology, 43(3), 1374-1390. https://doi.org/10.3390/cimb43030098
Nzuza, Nomfundo, et al. "Diversification of Ferredoxins across Living Organisms." Current issues in molecular biology vol. 43,3 (2021): 1374-1390. doi: https://doi.org/10.3390/cimb43030098
Nzuza N, Padayachee T, Chen W, Gront D, Nelson DR, Syed K. Diversification of Ferredoxins across Living Organisms. Curr Issues Mol Biol. 2021 Sep 30;43(3):1374-1390. doi: 10.3390/cimb43030098. PMID: 34698119.
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Rice Ferredoxins localize to chloroplasts/plastids and may function in different tissues.

Plant signaling & behavior

He L, Li M, Chen D, Qian Q, Zeng D, Zhu L.
PMID: 33989104
Plant Signal Behav. 2021 Sep 02;16(9):1926813. doi: 10.1080/15592324.2021.1926813. Epub 2021 May 14.

Ferredoxins (Fds) play a unique and important role in photosynthetic electron transport. Recently, we characterized the function of Fd1 in rice (

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He L, Li M, Chen D, et al. Rice Ferredoxins localize to chloroplasts/plastids and may function in different tissues. Plant Signal Behav. 2021;16(9):1926813doi: 10.1080/15592324.2021.1926813.
He, L., Li, M., Chen, D., Qian, Q., Zeng, D., & Zhu, L. (2021). Rice Ferredoxins localize to chloroplasts/plastids and may function in different tissues. Plant signaling & behavior, 16(9), 1926813. https://doi.org/10.1080/15592324.2021.1926813
He, Lei, et al. "Rice Ferredoxins localize to chloroplasts/plastids and may function in different tissues." Plant signaling & behavior vol. 16,9 (2021): 1926813. doi: https://doi.org/10.1080/15592324.2021.1926813
He L, Li M, Chen D, Qian Q, Zeng D, Zhu L. Rice Ferredoxins localize to chloroplasts/plastids and may function in different tissues. Plant Signal Behav. 2021 Sep 02;16(9):1926813. doi: 10.1080/15592324.2021.1926813. Epub 2021 May 14. PMID: 33989104; PMCID: PMC8281090.
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Showing 1 to 12 of 45 entries