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 11-14-2017, 04:20 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,951
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 A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation

A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation


Metalloproteins utilize O2 as an oxidant, and they often achieve a 4-electron reduction without H2O2 or oxygen radical release. Several proteins have been designed to catalyze one or two-electron oxidative chemistry, but the de novo design of a protein that catalyzes the net 4-electron reduction of O2 has not been reported yet. We report the construction of a diiron-binding four-helix bundle, made up of two different covalently linked ?2 monomers, through click chemistry. Surprisingly, the prototype protein, DF-C1, showed a large divergence in its reactivity from earlier DFs (DF: due ferri, two iron). DFs release the quinone imine and free H2O2 in the oxidation of 4-aminophenol in the presence of O2, whereas FeIII-DF-C1 sequesters the quinone imine into the active site, and catalyzes inside the scaffold an oxidative coupling between oxidized and reduced 4-aminophenol. The asymmetry of the scaffold allowed a fine-engineering of the substrate binding pocket, that ensures selectivity.Not just a four-helix bundle: The use of a diiron-binding four-helix bundle scaffold with an asymmetric active site leads to an enhancement in selectivity of the iron-catalyzed oxidative coupling of phenols. The stabilization of the oxidized intermediate in the binding pocket enables the net four-electron O2 reduction, without release of any detectable H2O2.

More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-dependent Oxidation
A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-dependent Oxidation Metalloproteins utilize O? as an oxidant, and they often achieve a 4-electron reduction without H?O? or oxygen radical release. Several proteins have been designed to catalyze one or two-electron oxidative chemistry, but the de novo design of a protein that catalyzes the net 4-electron reduction of O? has not been reported yet. We report here the construction of a diiron-binding four-helix bundle, made up of two different covalently linked ?2 monomers, through click...
nmrlearner Journal club 0 10-21-2017 04:46 AM
Salt-dependent and protein-concentration-dependent changes i
Salt-dependent and protein-concentration-dependent changes i More...
nmrlearner General 0 10-15-2013 09:48 PM
Protein lysine-N? alkylation and O-phosphorylation mediated by DTT-generated reactive oxygen species
Protein lysine-N? alkylation and O-phosphorylation mediated by DTT-generated reactive oxygen species Abstract Reactive oxygen species (ROS) play crucial roles in physiology and pathology. In this report, we use NMR spectroscopy and mass spectrometry (MS) to demonstrate that proteins (galectin-1, ubiquitin, RNase, cytochrome c, myoglobin, and lysozyme) under reducing conditions with dithiothreitol (DTT) become alkylated at lysine-N? groups and O-phosphorylated at serine and threonine residues. These adduction reactions only occur in the presence of monophosphate, potassium, trace metals...
nmrlearner Journal club 0 02-03-2013 09:54 AM
[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement. Related Articles An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement. J Am Chem Soc. 2005 Apr 27;127(16):5826-32 Authors: Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] NMR solution structure of a highly stable de novo heterodimeric coiled-coil.
NMR solution structure of a highly stable de novo heterodimeric coiled-coil. Related Articles NMR solution structure of a highly stable de novo heterodimeric coiled-coil. Biopolymers. 2004 Dec 5;75(5):367-75 Authors: Lindhout DA, Litowski JR, Mercier P, Hodges RS, Sykes BD The NMR solution structure of a highly stable coiled-coil IAAL-E3/K3 has been solved. The E3/K3 coiled-coil is a 42-residue de novo designed coiled-coil comprising three heptad repeats per subunit, stabilized by hydrophobic contacts within the core and electrostatic...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] Evidence for oxidation-state-dependent conformational changes in human ferredoxin fro
Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy. Related Articles Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy. Biochemistry. 1998 Mar 17;37(11):3965-73 Authors: Xia B, Volkman BF, Markley JL Human ferredoxin belongs to the vertebrate ferredoxin family which includes bovine adrenodoxin. It is a small (13.8 kDa) acidic protein with a cluster. It functions as an electron...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Investigation of oxidation state-dependent conformational changes in Desulfovibrio vu
Investigation of oxidation state-dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-NMR spectra. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Investigation of oxidation state-dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-NMR spectra. FEBS Lett. 1996 Jul 1;389(2):203-9 Authors: Blanchard L, Blackledge MJ, Marion D, Guerlesquin F Two-dimensional...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] The use of 19F NMR in the study of protein alkylation by fluorinated reactive interme
The use of 19F NMR in the study of protein alkylation by fluorinated reactive intermediates. Related Articles The use of 19F NMR in the study of protein alkylation by fluorinated reactive intermediates. Adv Exp Med Biol. 1991;283:735-8 Authors: Harris JW, Anders MW
nmrlearner Journal club 0 08-21-2010 11:16 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 - 2017, 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 05:40 AM.


Map