BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 08-22-2010, 03:33 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,134
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o

Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.

Related Articles Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study.

J Biol Chem. 1994 Mar 18;269(11):8052-8

Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, Münck E, Moura JJ

Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit structure as isolated; M(r) approximately 6400 per subunit; 6 cysteine residues) containing one Fe3S4 cluster per alpha-subunit. The x-ray structure of FdII has revealed a disulfide bridge formed by Cys-18 and Cys-42 approximately 13 A away from the center of the cluster; moreover, the x-ray structure indicates that Cys-11 forms a disulfide bridge with a methanethiol. In the oxidized state, FdIIoxm the 1H NMR spectra, exhibit four low-field contact-shifted resonances at 29, 24, 18, and 15.5 ppm whereas the reduced state, FdIIR (S = 2), yields two features at +18.5 and -11 ppm. In the course of studying the redox behavior of FdII, we have discovered a stable intermediate, FdIIint, that yields 1H resonances at 24, 21.5, 21, and 14 ppm. This intermediate appears in the potential range where the cluster (E'0 approximately -130 mV) is reduced from the [Fe3S4]1+ to the [Fe3S4]0 state. FdIIint is observed during reductive titrations with dithionite or hydrogen/hydrogenase or after partial oxidation of FdIIR by 2,6-dichlorophenolindophenol or air. Our studies show that a total of three electrons per alpha-subunit are transferred to FdII. Our experiments demonstrate the absence of a methanethiol-Cys-11 linkage in our preparations, and we propose that two of the three electrons are used for the reduction of the disulfide bridge. Mössbauer (and EPR) studies show that the Fe3S4 cluster of FdIIint is at the same oxidation level as FdIIox, but indicate some changes in the exchange couplings among the three ferric sites. Our data suggest that the differences in the NMR and Mössbauer spectra of FdIIox and FdIIint result from conformational changes attending the breaking or formation of the disulfide bridge. The present study suggests that experiments be undertaken to explore an in vivo redox function for the disulfide bridge.

PMID: 8132528 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Selective inhibition of Src SH2 by a novel thiol-targeting tricarbonyl-modified inhib
Selective inhibition of Src SH2 by a novel thiol-targeting tricarbonyl-modified inhibitor and mechanistic analysis by (1)H/(13)C NMR spectroscopy. Related Articles Selective inhibition of Src SH2 by a novel thiol-targeting tricarbonyl-modified inhibitor and mechanistic analysis by (1)H/(13)C NMR spectroscopy. Bioorg Med Chem Lett. 2001 Jul 9;11(13):1665-9 Authors: Sundaramoorthi R, Siedem C, Vu CB, Dalgarno DC, Laird EC, Botfield MC, Combs AB, Adams SE, Yuan RW, Weigele M, Narula SS Detailed analysis of Src SH2 binding by peptides containing a...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] 13C NMR chemical shifts can predict disulfide bond formation.
13C NMR chemical shifts can predict disulfide bond formation. Related Articles 13C NMR chemical shifts can predict disulfide bond formation. J Biomol NMR. 2000 Oct;18(2):165-71 Authors: Sharma D, Rajarathnam K The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded)...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Biochemistry. 1995 Dec 5;34(48):15646-53 Authors: Lanzilotta WN, Holz RC, Seefeldt LC This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus t
1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure. Related Articles 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure. Biochemistry. 1995 Jan 17;34(2):600-10 Authors: Gorst CM, Yeh YH, Teng Q, Calzolai L, Zhou ZH, Adams MW, La Mar GN One- and two-dimensional 1H NMR...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. J Biomol NMR. 1994 May;4(3):411-32 Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o
Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study. Related Articles Thiol/disulfide formation associated with the redox activity of the cluster of Desulfovibrio gigas ferredoxin II. 1H NMR and Mössbauer spectroscopic study. J Biol Chem. 1994 Mar 18;269(11):8052-8 Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, Münck E, Moura JJ Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. Related Articles Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxidized and reduced Escherichia coli thioredoxin. J Biomol NMR. 1994 May;4(3):411-32 Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thi
pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR. Related Articles pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR. J Biol Chem. 1990 Feb 15;265(5):2768-74 Authors: Lommen A, Canters GW The kinetics of the deuteronation of one of the copper ligand histidines of the reduced Type I blue-copper protein amicyanin from Thiobacillus versutus was studied as a...
nmrlearner Journal club 0 08-21-2010 10:48 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This Thread:

Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 08:51 AM.


Map