Structural highlights
Function
RUBR_PYRFU Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
Publication Abstract from PubMed
Neutron crystallographic analyses at near-atomic resolution are presented for both reduced and oxidized forms of perdeuterated Pyrococcus furiosus rubredoxin, a small iron-sulfur redox protein with remarkable thermostability. Hydronium ions may play a key role in the protonation and charge-transfer processes associated with the oxidized and reduced forms of the protein. Picture: overall structure showing D(3) O(+) ions (red and gray molecules).
Near-Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes.,Cuypers MG, Mason SA, Blakeley MP, Mitchell EP, Haertlein M, Forsyth VT Angew Chem Int Ed Engl. 2013 Jan 14;52(3):1022-5. doi: 10.1002/anie.201207071., Epub 2012 Dec 6. PMID:23225503[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cuypers MG, Mason SA, Blakeley MP, Mitchell EP, Haertlein M, Forsyth VT. Near-Atomic Resolution Neutron Crystallography on Perdeuterated Pyrococcus furiosus Rubredoxin: Implication of Hydronium Ions and Protonation State Equilibria in Redox Changes. Angew Chem Int Ed Engl. 2013 Jan 14;52(3):1022-5. doi: 10.1002/anie.201207071., Epub 2012 Dec 6. PMID:23225503 doi:10.1002/anie.201207071
