Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature - PubMed (original) (raw)
. 1995 Jul 11;34(27):8788-95.
doi: 10.1021/bi00027a030.
Affiliations
- PMID: 7612619
- DOI: 10.1021/bi00027a030
Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature
C M Gorst et al. Biochemistry. 1995.
Abstract
The oxidized and reduced forms of the [4Fe-4S]-containing ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus, Pf, have been investigated by 1H nuclear magnetic resonance spectroscopy, electron paramagnetic resonance spectroscopy and thiol titrations. We have identified and isolated at Ambient temperature four distinct redox states for the [4Fe-4S] form of the ferredoxin. These states differ in the redox state of the cluster, which is coordinated by Cys 11, Asp 14, Cys 17, and Cys 56, and of a disulfide bridge between Cys 21 and Cys 48. The protein, as isolated under anaerobic conditions, designated 4Fe FdBred, contains the reduced cluster and two free thiols. The cluster, but not the thiols, is readily oxidized by brief exposure to O2 to yield 4Fe FdBOX. Prolonged O2 treatment (> 24 h at 30 degrees C) is required to generate the protein with a disulfide (4Fe FdAOX) while this fully oxidized form is readily converted by brief reduction with sodium dithionite to the protein with a reduced cluster and a disulfide (4Fe FdAred). Analyses of the magnitude and the number of hyperfine-shifted resonances in each of the four redox states are discussed.
Similar articles
- Effect of iron-sulfur cluster environment in modulating the thermodynamic properties and biological function of ferredoxin from Pyrococcus furiosus.
Brereton PS, Verhagen MF, Zhou ZH, Adams MW. Brereton PS, et al. Biochemistry. 1998 May 19;37(20):7351-62. doi: 10.1021/bi972864b. Biochemistry. 1998. PMID: 9585549 Free PMC article.
Cited by
- Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization.
Hasan MN, Kwakernaak C, Sloof WG, Hagen WR, Heering HA. Hasan MN, et al. J Biol Inorg Chem. 2006 Jul;11(5):651-62. doi: 10.1007/s00775-006-0117-6. Epub 2006 May 30. J Biol Inorg Chem. 2006. PMID: 16791647 - Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe-4S] cluster.
Rodrigues PM, Macedo AL, Goodfellow BJ, Moura I, Moura JJ. Rodrigues PM, et al. J Biol Inorg Chem. 2006 Apr;11(3):307-15. doi: 10.1007/s00775-005-0077-2. Epub 2006 Feb 2. J Biol Inorg Chem. 2006. PMID: 16453120 - MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress response.
Ding X, Lv ZM, Zhao Y, Min H, Yang WJ. Ding X, et al. Cell Stress Chaperones. 2008 Summer;13(2):239-46. doi: 10.1007/s12192-008-0026-4. Epub 2008 Feb 28. Cell Stress Chaperones. 2008. PMID: 18759006 Free PMC article. - Posttranslational protein modification in Archaea.
Eichler J, Adams MW. Eichler J, et al. Microbiol Mol Biol Rev. 2005 Sep;69(3):393-425. doi: 10.1128/MMBR.69.3.393-425.2005. Microbiol Mol Biol Rev. 2005. PMID: 16148304 Free PMC article. Review. - Voltammetric studies of the reactions of iron-sulphur clusters ([3Fe-4S] or [M3Fe-4S]) formed in Pyrococcus furiosus ferredoxin.
Fawcett SE, Davis D, Breton JL, Thomson AJ, Armstrong FA. Fawcett SE, et al. Biochem J. 1998 Oct 15;335 ( Pt 2)(Pt 2):357-68. doi: 10.1042/bj3350357. Biochem J. 1998. PMID: 9761735 Free PMC article.