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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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  
Old 11-24-2010, 08:58 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 1H NMR structure of the heme pocket of HNO-myoglobin.

1H NMR structure of the heme pocket of HNO-myoglobin.

Related Articles 1H NMR structure of the heme pocket of HNO-myoglobin.

J Biol Inorg Chem. 2003 Feb;8(3):348-52

Authors: Sulc F, Fleischer E, Farmer PJ, Ma D, La Mar GN

The unique (1)H NMR signal of nitrosyl hydride at 14.8 ppm is used to obtain a solution structure of the distal pocket of Mb-HNO, a rare nitroxyl adduct with a half-life of several months at room temperature. (1)H NMR, NOESY and TOCSY data were obtained under identical experimental conditions on solutions of the diamagnetic HNO and CO complexes of equine Mb, allowing direct comparison of NMR data to a crystallographically characterized structure. Twenty NOEs between the nitrosyl hydride and protein and heme-based signals were observed. The HNO orientation obtained by modeling the experimental (1)H NMR NOESY data yielded an orientation of ca. -104 degrees referenced to the N-Fe-N vector between alpha and beta mesoprotons. An essentially identical orientation was obtained by simple energy minimization of the HNO adduct using ESFF potentials, suggesting steric control of the orientation. Differences in chemical shifts are seen for protons on residues Phe43(CD1) and Val68(E11), but both exhibit virtually identical NOESY contacts to other residues, and thus are attributed to small movements of ca. 0.1 A within the strong ring current. The most significant differences are seen in the NOESY peak intensities and chemical shifts for the ring non-labile protons of the distal His64(E7). The orientation of the His64(E7) in Mb-HNO was analyzed on the basis of the NOESY cross-peak changes and chemical shift changes, predicting a ca. 20 degrees rotation about the beta-gamma bond. The deduced HNO and His64(E7) orientations result in geometry where the His64(E7) ring can serve as the donor for a significant H-bond to the oxygen atom of the bound HNO.

PMID: 12589571 [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
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin. Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin. Biochim Biophys Acta. 2011 May 6; Authors: Juillard S, Chevance S, Bondon A, Simonneaux G The asymmetric 3-ethyl-2-methylporphyrin iron complex was synthetized and inserted into apomyoglobin. UV-visible spectroscopic studies demonstrated the capacity of iron to coordinate different exogenous axial ligands in ferrous and...
nmrlearner Journal club 0 05-24-2011 12:00 PM
[NMR paper] NMR structure of the thromboxane A2 receptor ligand recognition pocket.
NMR structure of the thromboxane A2 receptor ligand recognition pocket. Related Articles NMR structure of the thromboxane A2 receptor ligand recognition pocket. Eur J Biochem. 2004 Jul;271(14):3006-16 Authors: Ruan KH, Wu J, So SP, Jenkins LA, Ruan CH To overcome the difficulty of characterizing the structures of the extracellular loops (eLPs) of G protein-coupled receptors (GPCRs) other than rhodopsin, we have explored a strategy to generate a three-dimensional structural model for a GPCR, the thromboxane A(2) receptor. This three-dimensional...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Two-dimensional NMR study of the heme active site structure of chloroperoxidase. Related Articles Two-dimensional NMR study of the heme active site structure of chloroperoxidase. J Biol Chem. 2003 Mar 7;278(10):7765-74 Authors: Wang X, Tachikawa H, Yi X, Manoj KM, Hager LP The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays versatile catalytic activities isolated from the marine mold Caldariomyces fumago, has been characterized by two-dimensional NMR spectroscopic studies. All hyperfine shifted resonances...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Two-dimensional NMR characterization of the deoxymyoglobin heme pocket. Related Articles Two-dimensional NMR characterization of the deoxymyoglobin heme pocket. Biochemistry. 1994 Sep 13;33(36):10934-43 Authors: Busse SC, Jue T Traditionally, assigning the heme protein resonances has relied heavily on the comparison of spectra arising from protein reconstituted with specifically deuterated hemes and the native form. Such an approach can identify tentatively the broad, overlapping signals in the Fe(II) high-spin heme protein spectra. Although...
nmrlearner Journal club 0 08-22-2010 03:29 AM
[NMR paper] 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. Eur J Biochem. 1993 Jul 15;215(2):431-7 Authors: Banci L, Bertini I, Marconi S, Pierattelli R The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket st
1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Related Articles 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Biochemistry. 1991 Feb 19;30(7):1878-87 Authors: Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM 1H nuclear magnetic resonance spectroscopy was used to assign the hyperfine-shifted resonances and determine the position of...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] Characterization by NMR of the heme-myoglobin adduct formed during the reductive meta
Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group. Related Articles Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group. J Biol Chem. 1991 Feb 15;266(5):3208-14 Authors: Osawa Y, Highet RJ, Bax A, Pohl LR The reductive debromination of BrCCl3 by ferrous deoxymyoglobin leads to the covalent bonding of the...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] 1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorh
1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of heme propanoate mobility in the active site of myoglobin from Galeorhinus japonicus. Eur J Biochem. 1990 May 20;189(3):567-73 Authors: Yamamoto Y, Inoue Y, Chûjô R, Suzuki T Time-dependent NOE studies of the C13(1) and C17(1) methylene proton resonances of the heme...
nmrlearner Journal club 0 08-21-2010 10:48 PM



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 06:49 AM.


Map