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, 02:27 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,135
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 C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacety

C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.

Related Articles C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.

J Biochem. 1996 Mar;119(3):512-9

Authors: Miura R, Nishina Y, Fuji S, Shiga K

The change-transfer interaction in the complex of pig kidney medium-chain acyl-CoA dehydrogenase (MCAD) with acetoacetyl-CoA was investigated by 13C-NMR spectroscopy and molecular orbital treatment. The acyl carbons of acetoacetyl-CoA were separately 13C-labeled and 13C-NMR spectra of the complexes of MCAD with the 13C-labeled acetoacetyl-CoA were measured. Each 13C-carbon atom was observed as a distinct peak and easily distinguished from the protein background. The chemical shift values for free acetoacetyl-CoA were 198.5, 59.9, 208.8, and 32.8 ppm for C(1), C(2), C(3), and C(4), respectively, which shifted to 181.3, 103.4, 192.3, and 29.9 ppm, respectively, when acetoacetyl-CoA was complexed with MCAD. While C(4) underwent a small upfield shift, the other carbons complexed with MCAD. While C(4) underwent a small upfield shift, the other carbons experienced significant shifts; both the C(1) and C(3) carbonyl carbons shifted upfield by about 17 ppm, and the C(2) carbon was observed as a very broad peak at a position shifted downfield by more than 40 ppm. These results were compared with 13C-NMR spectra of the keto-, enol-, and enolate forms of ethyl acetoacetate labeled with 13C at the acyl carbons, and interpreted with reference to the charge-transfer model based on the optimum overlap between the lowest unoccupied molecular orbital (LUMO) of flavin and the highest occupied molecular orbital (HOMO) of the enolate state of the acetoacetyl moiety of acetoacetyl-CoA. The C(2) carbon of acetoacetyl-CoA takes on the sp2 configuration in the bound form, indicating that one of the protons at C(2) of acetoacetyl-CoA is abstracted when bound to MCAD. C(1) = O is substantially polarized in the bound form of acetoacetyl-CoA, implying the presence of a machinery that polarizes this carbonyl group at the binding site, which thereby lowers the pKa value of the alpha-proton at C(2). This machinery is of fundamental importance in the initial step of MCAD catalysis.

PMID: 8830047 [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] Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase reveal
Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy. Related Articles Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase revealed by NMR spectroscopy. J Am Chem Soc. 2005 Jun 15;127(23):8424-32 Authors: Wu J, Bell AF, Jaye AA, Tonge PJ Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. The interaction of hexadienoyl-CoA (HD-CoA), a product analogue, with recombinant pig...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I i
Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I incorporated into the active site of cyano-metmyoglobin. Related Articles Solution 1H NMR study of the accommodation of the side chain of n-butyl-etiohemin-I incorporated into the active site of cyano-metmyoglobin. J Biol Inorg Chem. 2005 May;10(3):283-93 Authors: Bondarenko V, Wang J, Kalish H, Balch AL, La Mar GN In order to identify the most readily deformable portion of the heme pocket in myoglobin, equine myoglobin was reconstituted with a meso-n-butyl...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme com
Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy. Related Articles Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy. FEBS J. 2005 Jan;272(1):259-68 Authors: Allen MD, Broadhurst RW, Solomon RG, Perham RN A (15)N-labelled peripheral-subunit binding domain (PSBD) of the dihydrolipoyl...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Detection of very weak side chain-main chain hydrogen bonding interactions in medium-
Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy. Related Articles Detection of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled proteins by sensitivity-enhanced NMR spectroscopy. J Biomol NMR. 2000 May;17(1):79-82 Authors: Liu A, Hu W, Majumdar A, Rosen MK, Patel DJ We describe the direct observation of very weak side chain-main chain hydrogen bonding interactions in medium-size 13C/15N-labeled...
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
13C NMR studies of the binding of medium-chain fatty acids to human serum albumin. Related Articles 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin. J Lipid Res. 1994 Mar;35(3):458-67 Authors: Kenyon MA, Hamilton JA Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin.
13C NMR studies of the binding of medium-chain fatty acids to human serum albumin. Related Articles 13C NMR studies of the binding of medium-chain fatty acids to human serum albumin. J Lipid Res. 1994 Mar;35(3):458-67 Authors: Kenyon MA, Hamilton JA Binding of the medium-chain fatty acids (MCFA), octanoic (OCT) and decanoic (DEC) acid, to human serum albumin (HSA) has been studied by 13C NMR spectroscopy. NMR spectra at 35 degrees C showed an apparently homogeneous binding environment (a single, narrow resonance for the 13C-enriched carboxyl...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escheric
A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli. Protein Sci. 1993 Nov;2(11):1938-47 Authors: Sun ZY, Truong HT, Pratt EA, Sutherland DC,...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of col
Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of colloidal properties of dihexanoyl phosphatidylcholine. Related Articles Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of colloidal properties of dihexanoyl phosphatidylcholine. Chem Phys Lipids. 1990 Sep;55(3):351-4 Authors: Eisele JL, Neumann JM, Chachaty C The colloidal features of short chain phospholipids can be deduced from 31P-NMR analysis by comparison with available data on phospholipid aqueous dispersion. In this study...
nmrlearner Journal club 0 08-21-2010 11:04 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 07:37 AM.


Map