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Crystal structure of the [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii.

Acta crystallographica. Section F, Structural biology communications

Kabasakal BV, Cotton CAR, Murray JW.
PMID: 34726179
Acta Crystallogr F Struct Biol Commun. 2021 Nov 01;77:407-411. doi: 10.1107/S2053230X21009936. Epub 2021 Oct 19.

Azotobacter vinelandii is a model diazotroph and is the source of most nitrogenase material for structural and biochemical work. Azotobacter can grow in above-atmospheric levels of oxygen, despite the sensitivity of nitrogenase activity to oxygen. Azotobacter has many iron-sulfur...

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Kabasakal BV, Cotton CAR, Murray JW. Crystal structure of the [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii. Acta Crystallogr F Struct Biol Commun. 2021;77:407-411doi: 10.1107/S2053230X21009936.
Kabasakal, B. V., Cotton, C. A. R., & Murray, J. W. (2021). Crystal structure of the [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii. Acta crystallographica. Section F, Structural biology communications, 77407-411. https://doi.org/10.1107/S2053230X21009936
Kabasakal, Burak V, et al. "Crystal structure of the [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii." Acta crystallographica. Section F, Structural biology communications vol. 77 (2021): 407-411. doi: https://doi.org/10.1107/S2053230X21009936
Kabasakal BV, Cotton CAR, Murray JW. Crystal structure of the [2Fe-2S] protein I (Shethna protein I) from Azotobacter vinelandii. Acta Crystallogr F Struct Biol Commun. 2021 Nov 01;77:407-411. doi: 10.1107/S2053230X21009936. Epub 2021 Oct 19. PMID: 34726179; PMCID: PMC8561814.
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Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin.

Chemical communications (Cambridge, England)

Scintilla S, Bonfio C, Belmonte L, Forlin M, Rossetto D, Li J, Cowan JA, Galliani A, Arnesano F, Assfalg M, Mansy SS.
PMID: 27790655
Chem Commun (Camb). 2016 Nov 10;52(92):13456-13459. doi: 10.1039/c6cc07912a.

Based on UV-Vis, NMR, and EPR spectroscopies and DFT and molecular dynamics calculations, a model prebiotic [2Fe-2S] tripeptide was shown to accept and donate electrons. Duplications of the tripeptide sequence led to a protoferredoxin with increased stability. Duplications of...

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Scintilla S, Bonfio C, Belmonte L, et al. Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin. Chem Commun (Camb). 2016;52(92):13456-13459doi: 10.1039/c6cc07912a.
Scintilla, S., Bonfio, C., Belmonte, L., Forlin, M., Rossetto, D., Li, J., Cowan, J. A., Galliani, A., Arnesano, F., Assfalg, M., & Mansy, S. S. (2016). Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin. Chemical communications (Cambridge, England), 52(92), 13456-13459. https://doi.org/10.1039/c6cc07912a
Scintilla, Simone, et al. "Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin." Chemical communications (Cambridge, England) vol. 52,92 (2016): 13456-13459. doi: https://doi.org/10.1039/c6cc07912a
Scintilla S, Bonfio C, Belmonte L, Forlin M, Rossetto D, Li J, Cowan JA, Galliani A, Arnesano F, Assfalg M, Mansy SS. Duplications of an iron-sulphur tripeptide leads to the formation of a protoferredoxin. Chem Commun (Camb). 2016 Nov 10;52(92):13456-13459. doi: 10.1039/c6cc07912a. PMID: 27790655.
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Individual Reduction Potentials of the Iron Ions in Fe(2)S(2) and High-Potential Fe(4)S(4) Ferredoxins.

Inorganic chemistry

Banci L, Bertini I, Gori Savellini G, Luchinat C.
PMID: 11666635
Inorg Chem. 1996 Jul 03;35(14):4248-4253. doi: 10.1021/ic960051q.

The DelPhi program package has been used to confirm that the span in reduction potentials among high-potential Fe(4)S(4) ferredoxins must be mainly ascribed to the net protein charges arising from acidic and basic residues. Subsequently, the order of the...

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Banci L, Bertini I, Gori Savellini G, et al. Individual Reduction Potentials of the Iron Ions in Fe(2)S(2) and High-Potential Fe(4)S(4) Ferredoxins. Inorg Chem. 1996;35(14):4248-4253doi: 10.1021/ic960051q.
Banci, L., Bertini, I., Gori Savellini, G., & Luchinat, C. (1996). Individual Reduction Potentials of the Iron Ions in Fe(2)S(2) and High-Potential Fe(4)S(4) Ferredoxins. Inorganic chemistry, 35(14), 4248-4253. https://doi.org/10.1021/ic960051q
Banci, Lucia, et al. "Individual Reduction Potentials of the Iron Ions in Fe(2)S(2) and High-Potential Fe(4)S(4) Ferredoxins." Inorganic chemistry vol. 35,14 (1996): 4248-4253. doi: https://doi.org/10.1021/ic960051q
Banci L, Bertini I, Gori Savellini G, Luchinat C. Individual Reduction Potentials of the Iron Ions in Fe(2)S(2) and High-Potential Fe(4)S(4) Ferredoxins. Inorg Chem. 1996 Jul 03;35(14):4248-4253. doi: 10.1021/ic960051q. PMID: 11666635.
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The evolution of ferredoxins.

Trends in ecology & evolution

Meyer J.
PMID: 21227235
Trends Ecol Evol. 1988 Sep;3(9):222-6. doi: 10.1016/0169-5347(88)90162-0.

Ferredoxins are electron carrier proteins that contain active sites consisting of nonheme iron and inorganic sulfur. They are ubiquitous in living cells and are believed to be among the earliest redox proteins having appeared in primitive organisms. The small...

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Meyer J. The evolution of ferredoxins. Trends Ecol Evol. 1988;3(9):222-6doi: 10.1016/0169-5347(88)90162-0.
Meyer, J. (1988). The evolution of ferredoxins. Trends in ecology & evolution, 3(9), 222-6. https://doi.org/10.1016/0169-5347(88)90162-0
Meyer, J. "The evolution of ferredoxins." Trends in ecology & evolution vol. 3,9 (1988): 222-6. doi: https://doi.org/10.1016/0169-5347(88)90162-0
Meyer J. The evolution of ferredoxins. Trends Ecol Evol. 1988 Sep;3(9):222-6. doi: 10.1016/0169-5347(88)90162-0. PMID: 21227235.
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The coding site of chloroplast ferredoxin.

Planta

Huisman JG, Gebbink MG, Modderman P, Stegwee D.
PMID: 24420625
Planta. 1977 Jan;137(2):97-105. doi: 10.1007/BF00387545.

Ferredoxins were isolated and purified from leaves of different species of Nicotiana and Petunia and from spinach leaves. Their spectral properties, degree of homogeneity, and molecular weights were determined. The preparations were further analyzed by polyacrylamide gel electrophoresis of...

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Huisman JG, Gebbink MG, Modderman P, et al. The coding site of chloroplast ferredoxin. Planta. 1977;137(2):97-105doi: 10.1007/BF00387545.
Huisman, J. G., Gebbink, M. G., Modderman, P., & Stegwee, D. (1977). The coding site of chloroplast ferredoxin. Planta, 137(2), 97-105. https://doi.org/10.1007/BF00387545
Huisman, J G, et al. "The coding site of chloroplast ferredoxin." Planta vol. 137,2 (1977): 97-105. doi: https://doi.org/10.1007/BF00387545
Huisman JG, Gebbink MG, Modderman P, Stegwee D. The coding site of chloroplast ferredoxin. Planta. 1977 Jan;137(2):97-105. doi: 10.1007/BF00387545. PMID: 24420625.
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Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation.

Photosynthesis research

Van Der Plas J, De Groot R, Woortman M, Cremers F, Borrias M, Van Arkel G, Weisbeek P.
PMID: 24425165
Photosynth Res. 1988 Oct;18(1):179-204. doi: 10.1007/BF00042984.

The gene encoding ferredoxin I (petF1) from the filamentous cyanobacterium Anabaena sp. PCC 7937 (Anabaena variabilis ATCC 29413) was cloned by low stringency hybridization with the ferredoxin cDNA from the higher plant Silene pratensis. The petF1 gene from the...

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Van Der Plas J, De Groot R, Woortman M, et al. Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation. Photosynth Res. 1988;18(1):179-204doi: 10.1007/BF00042984.
Van Der Plas, J., De Groot, R., Woortman, M., Cremers, F., Borrias, M., Van Arkel, G., & Weisbeek, P. (1988). Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation. Photosynthesis research, 18(1), 179-204. https://doi.org/10.1007/BF00042984
Van Der Plas, J, et al. "Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation." Photosynthesis research vol. 18,1 (1988): 179-204. doi: https://doi.org/10.1007/BF00042984
Van Der Plas J, De Groot R, Woortman M, Cremers F, Borrias M, Van Arkel G, Weisbeek P. Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation. Photosynth Res. 1988 Oct;18(1):179-204. doi: 10.1007/BF00042984. PMID: 24425165.
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Cs8[Fe4S10] and Cs7[Fe4S8], two new sulfido ferrates with different tetrameric anions.

Inorganic chemistry

Schwarz M, Röhr C.
PMID: 25514465
Inorg Chem. 2015 Feb 02;54(3):1038-48. doi: 10.1021/ic502382v. Epub 2014 Dec 16.

The two new cesium sulfido ferrates Cs(8)[Fe(4)S(10)] and Cs(7)[Fe(4)S(8)] were synthesized at a maximum temperature of 1070 K in corundum crucibles from stoichiometric samples containing elemental Fe and S together with cesium disulfide, Cs(2)S(2). Their crystal structures have been...

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Schwarz M, Röhr C. Cs8[Fe4S10] and Cs7[Fe4S8], two new sulfido ferrates with different tetrameric anions. Inorg Chem. 2014;54(3):1038-48doi: 10.1021/ic502382v.
Schwarz, M., & Röhr, C. (2015). Cs8[Fe4S10] and Cs7[Fe4S8], two new sulfido ferrates with different tetrameric anions. Inorganic chemistry, 54(3), 1038-48. https://doi.org/10.1021/ic502382v
Schwarz, Michael, and Röhr, Caroline. "Cs8[Fe4S10] and Cs7[Fe4S8], two new sulfido ferrates with different tetrameric anions." Inorganic chemistry vol. 54,3 (2015): 1038-48. doi: https://doi.org/10.1021/ic502382v
Schwarz M, Röhr C. Cs8[Fe4S10] and Cs7[Fe4S8], two new sulfido ferrates with different tetrameric anions. Inorg Chem. 2015 Feb 02;54(3):1038-48. doi: 10.1021/ic502382v. Epub 2014 Dec 16. PMID: 25514465.
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Amino acid sequence of ferredoxin II from the phototroph Rhodospirillum rubrum: Characteristics of a 7Fe ferredoxin.

Photosynthesis research

Ishikawa Y, Yoch DC.
PMID: 24301605
Photosynth Res. 1995 Nov;46(1):371-6. doi: 10.1007/BF00020453.

The complete sequence of amino acids of ferredoxin II (FdII) from Rhodospirillum rubrum was determined by repetitive Edman degradation using pyridylethylated-ferredoxin and oxidized, denatured ferredoxin. Peptides derived from trypsin, pepsin, Glu-C endoproteinase, Arg-C endoproteinase, tryptophan specific cleavage and partial...

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Ishikawa Y, Yoch DC. Amino acid sequence of ferredoxin II from the phototroph Rhodospirillum rubrum: Characteristics of a 7Fe ferredoxin. Photosynth Res. 1995;46(1):371-6doi: 10.1007/BF00020453.
Ishikawa, Y., & Yoch, D. C. (1995). Amino acid sequence of ferredoxin II from the phototroph Rhodospirillum rubrum: Characteristics of a 7Fe ferredoxin. Photosynthesis research, 46(1), 371-6. https://doi.org/10.1007/BF00020453
Ishikawa, Y, and Yoch, D C. "Amino acid sequence of ferredoxin II from the phototroph Rhodospirillum rubrum: Characteristics of a 7Fe ferredoxin." Photosynthesis research vol. 46,1 (1995): 371-6. doi: https://doi.org/10.1007/BF00020453
Ishikawa Y, Yoch DC. Amino acid sequence of ferredoxin II from the phototroph Rhodospirillum rubrum: Characteristics of a 7Fe ferredoxin. Photosynth Res. 1995 Nov;46(1):371-6. doi: 10.1007/BF00020453. PMID: 24301605.
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Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria.

Chemical science

Child SA, Bradley JM, Pukala TL, Svistunenko DA, Le Brun NE, Bell SG.
PMID: 30542550
Chem Sci. 2018 Aug 23;9(41):7948-7957. doi: 10.1039/c8sc01286e. eCollection 2018 Nov 07.

The proteins responsible for controlling electron transfer in bacterial secondary metabolism are not always known or characterised. Here we demonstrate that many bacteria contain a set of unfamiliar ferredoxin encoding genes which are associated with those of cytochrome P450...

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Child SA, Bradley JM, Pukala TL, et al. Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria. Chem Sci. 2018;9(41):7948-7957doi: 10.1039/c8sc01286e.
Child, S. A., Bradley, J. M., Pukala, T. L., Svistunenko, D. A., Le Brun, N. E., & Bell, S. G. (2018). Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria. Chemical science, 9(41), 7948-7957. https://doi.org/10.1039/c8sc01286e
Child, Stella A, et al. "Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria." Chemical science vol. 9,41 (2018): 7948-7957. doi: https://doi.org/10.1039/c8sc01286e
Child SA, Bradley JM, Pukala TL, Svistunenko DA, Le Brun NE, Bell SG. Electron transfer ferredoxins with unusual cluster binding motifs support secondary metabolism in many bacteria. Chem Sci. 2018 Aug 23;9(41):7948-7957. doi: 10.1039/c8sc01286e. eCollection 2018 Nov 07. PMID: 30542550; PMCID: PMC6237146.
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The Transfer of the Ferredoxin Gene From the Chloroplast to the Nuclear Genome Is Ancient Within the Paraphyletic Genus .

Frontiers in microbiology

Roy AS, Woehle C, LaRoche J.
PMID: 33123095
Front Microbiol. 2020 Oct 02;11:523689. doi: 10.3389/fmicb.2020.523689. eCollection 2020.

Ferredoxins are iron-sulfur proteins essential for a wide range of organisms because they are an electron transfer mediator involved in multiple metabolic pathways. In phytoplankton, these proteins are active in the mature chloroplasts, but the

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Roy AS, Woehle C, LaRoche J. The Transfer of the Ferredoxin Gene From the Chloroplast to the Nuclear Genome Is Ancient Within the Paraphyletic Genus . Front Microbiol. 2020;11:523689doi: 10.3389/fmicb.2020.523689.
Roy, A. S., Woehle, C., & LaRoche, J. (2020). The Transfer of the Ferredoxin Gene From the Chloroplast to the Nuclear Genome Is Ancient Within the Paraphyletic Genus . Frontiers in microbiology, 11523689. https://doi.org/10.3389/fmicb.2020.523689
Roy, Alexandra-Sophie, et al. "The Transfer of the Ferredoxin Gene From the Chloroplast to the Nuclear Genome Is Ancient Within the Paraphyletic Genus ." Frontiers in microbiology vol. 11 (2020): 523689. doi: https://doi.org/10.3389/fmicb.2020.523689
Roy AS, Woehle C, LaRoche J. The Transfer of the Ferredoxin Gene From the Chloroplast to the Nuclear Genome Is Ancient Within the Paraphyletic Genus . Front Microbiol. 2020 Oct 02;11:523689. doi: 10.3389/fmicb.2020.523689. eCollection 2020. PMID: 33123095; PMCID: PMC7566914.
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Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution.

Acta crystallographica. Section D, Biological crystallography

TranQui D, Jésior JC.
PMID: 15299316
Acta Crystallogr D Biol Crystallogr. 1995 Mar 01;51:155-9. doi: 10.1107/S0907444994010735.

Ferredoxins (Fd) are electron-carrier proteins, the active sites of which are organized around clusters made of iron and inorganic sulfur. The Fd from Clostridium acidurici is 55 amino acids long and contains two [4Fe-4S] clusters. Crystals have been obtained...

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TranQui D, Jésior JC. Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1995;51:155-9doi: 10.1107/S0907444994010735.
TranQui, D., & Jésior, J. C. (1995). Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution. Acta crystallographica. Section D, Biological crystallography, 51155-9. https://doi.org/10.1107/S0907444994010735
TranQui, D, and Jésior, J C. "Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution." Acta crystallographica. Section D, Biological crystallography vol. 51 (1995): 155-9. doi: https://doi.org/10.1107/S0907444994010735
TranQui D, Jésior JC. Structure of the ferredoxin from Clostridium acidurici: model at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Mar 01;51:155-9. doi: 10.1107/S0907444994010735. PMID: 15299316.
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The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters.

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

Bruice TC, Maskiewicz R, Job R.
PMID: 16592211
Proc Natl Acad Sci U S A. 1975 Jan;72(1):231-4. doi: 10.1073/pnas.72.1.231.

The iron-sulfur cluster compounds Fe(4)S(4)(SR)(4) (-2) [where -SR = -SCH(3), -S-C(CH(3))(3), and -S- CH(2)-CH(CH(3))(2)] have been found to represent the base species of weak acids of pK(a) comparable to that of carboxylic acids. The acid species Fe(4)S(4)(SR)(4)H(-) is most...

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Bruice TC, Maskiewicz R, Job R. The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters. Proc Natl Acad Sci U S A. 1975;72(1):231-4doi: 10.1073/pnas.72.1.231.
Bruice, T. C., Maskiewicz, R., & Job, R. (1975). The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters. Proceedings of the National Academy of Sciences of the United States of America, 72(1), 231-4. https://doi.org/10.1073/pnas.72.1.231
Bruice, T C, et al. "The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters." Proceedings of the National Academy of Sciences of the United States of America vol. 72,1 (1975): 231-4. doi: https://doi.org/10.1073/pnas.72.1.231
Bruice TC, Maskiewicz R, Job R. The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters. Proc Natl Acad Sci U S A. 1975 Jan;72(1):231-4. doi: 10.1073/pnas.72.1.231. PMID: 16592211; PMCID: PMC432277.
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Showing 13 to 24 of 45 entries