Rubredoxin: Difference between revisions
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been implicated as functional entities in electron transport in mitochondria from mammalian tissue. Rubredoxin is a distinct class of | been implicated as functional entities in electron transport in mitochondria from mammalian tissue. Rubredoxin is a distinct class of | ||
electron transfer proteins because of its striking feature of the lack of an inorganic sulfide. <ref>Calderon, R. H., García-Cerdán, J. G., Malnoë, A., Cook, R., Russell, J. J., Gaw, C., Dent, R. M., de Vitry, C., & Niyogi, K. K. (2013, September 13). A conserved rubredoxin is necessary for photosystem II accumulation in diverse oxygenic photoautotrophs. The Journal of biological chemistry. Retrieved April 21, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772215/ </ref> | electron transfer proteins because of its striking feature of the lack of an inorganic sulfide. <ref>Calderon, R. H., García-Cerdán, J. G., Malnoë, A., Cook, R., Russell, J. J., Gaw, C., Dent, R. M., de Vitry, C., & Niyogi, K. K. (2013, September 13). A conserved rubredoxin is necessary for photosystem II accumulation in diverse oxygenic photoautotrophs. The Journal of biological chemistry. Retrieved April 21, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772215/ </ref> | ||
== Function == | == Function == | ||
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</ref> | </ref> | ||
A study was done to figure out how the protein environment influences the electron transfer properties of its redox site and what underlying structural features are responsible for the redox reaction. Based on the two 1.5 Å resolution structures, an electron would be transferred from an electron donor protein to an oxidized rubredoxin, which would result in a reduced rubredoxin. The reduced rubredoxin could be stabilized by the transient entry of water through the gate. Next, the stabilized reduced rubredoxin could diffuse to a partner electron-acceptor protein. <ref>Libretexts. (2020, August 10). 7.12: Rubredoxin- a single-fe tetrathiolate protein. Chemistry LibreTexts. Retrieved April 21, 2022, from https://chem.libretexts.org/Bookshelves/Inorganic_Chemistry/Book3A_Bioinorganic_Chemistry_(Bertini_et_al.)/07%3A_Ferrodoxins_Hydrogenases_and_Nitrogenases_-_Metal-Sulfide_Proteins/7.12%3A_Rubredoxin-_A_Single-Fe_Tetrathiolate_Protein</ref> If the acceptor protein-bound while the gate is closed and no water is present in a manner that makes it difficult for the gate to open, the reduced rubredoxin would be kept in the less stable state without the water. This would favor electron transfer to the acceptor protein, which could occur through the exposed Cys 42 Sγ. | A study was done to figure out how the protein environment influences the electron transfer properties of its redox site and what underlying structural features are responsible for the redox reaction. Based on the two 1.5 Å resolution structures, an electron would be transferred from an electron donor protein to an oxidized rubredoxin, which would result in a reduced rubredoxin. The reduced rubredoxin could be stabilized by the transient entry of water through the gate. Next, the stabilized reduced rubredoxin could diffuse to a partner electron-acceptor protein. <ref>Libretexts. (2020, August 10). 7.12: Rubredoxin- a single-fe tetrathiolate protein. Chemistry LibreTexts. Retrieved April 21, 2022, from https://chem.libretexts.org/Bookshelves/Inorganic_Chemistry/Book3A_Bioinorganic_Chemistry_(Bertini_et_al.)/07%3A_Ferrodoxins_Hydrogenases_and_Nitrogenases_-_Metal-Sulfide_Proteins/7.12%3A_Rubredoxin-_A_Single-Fe_Tetrathiolate_Protein</ref> If the acceptor protein-bound while the gate is closed and no water is present in a manner that makes it difficult for the gate to open, the reduced rubredoxin would be kept in the less stable state without the water. This would favor electron transfer to the acceptor protein, which could occur through the exposed Cys 42 Sγ. | ||
== Mechanism == | == Mechanism == | ||
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<scene name='90/909991/Rubredoxin_2/1'>At 1.6 angstroms</scene>, a neutron diffraction study has been carried out on a mutant rubredoxin from Pyrococcus furiosus. Three residues in this Pyrococcus furiosus mutation were changed (Trp3 → Tyr3, Ile23 → Val23, Leu32 → Ile32). There were also some changes that were found between the wild-type and mutant proteins in the Trp3/Tyr3 region. The N-H amide bonds of the protein backbone are important because they could contain information about the mechanism of unfolding of this small protein. The 1.6 A resolution of this neutron structure reveals some orders of the water structure such as the ordered and disordered O-D bonds. The total structure weight is 5.92 kDa with an atom count of 446. There is one unique protein chain and a deposited residue count of 51. | <scene name='90/909991/Rubredoxin_2/1'>At 1.6 angstroms</scene>, a neutron diffraction study has been carried out on a mutant rubredoxin from Pyrococcus furiosus. Three residues in this Pyrococcus furiosus mutation were changed (Trp3 → Tyr3, Ile23 → Val23, Leu32 → Ile32). There were also some changes that were found between the wild-type and mutant proteins in the Trp3/Tyr3 region. The N-H amide bonds of the protein backbone are important because they could contain information about the mechanism of unfolding of this small protein. The 1.6 A resolution of this neutron structure reveals some orders of the water structure such as the ordered and disordered O-D bonds. The total structure weight is 5.92 kDa with an atom count of 446. There is one unique protein chain and a deposited residue count of 51. | ||
==Rubredoxin 3D PDB structures== | |||
[[Rubredoxin PDB structures]] | |||
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||