Reaction Details  Report a problem with these data
Cell Reactant:
FAD-Binding Domain
Syringe Reactant:
BDBM11941
Meas. Tech.:
Isothermal Titration Calorimetry
Entry Date.:
2006-11-07
ΔG°:
-43.0540±n/a (kJ/mole)
pH:
7.0000±n/a
Log10Kb:
6.3
Temperature:
298.1500±n/a (K)
ΔHobs :
-79.4200±0.0000 (kJ/mole)
Corrected for ΔHioniz:
not known
ΔCp :
-1.2540±n/a (kJ/mole)
Stoich. Param.:
0.9000
ΔS° :
-0.1290±n/a (kJ/mole-K)
Citation
 Hoffman, JM; Grunau, A; Smith, AM; Paine, MJ; Rooney, CS; Ladbury, JE; Fisher, TE; Gutierrez, A; Wai, JS; Thomas, CM; Bamberger, DL; Barnes, JL; Williams, TM; Jones, JH Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase. Biochemistry 45:1421-34 (2006) [PubMed]  Article
Cell React
Source:
The functional FAD-binding domain, includes the linker region, of human fibroblast CPR was expressed in Escherichia coli BL21 (DE3).
Prep. Method:
The recombinant His-tagged proteins were purified to homogeneity by nickel-agarose chromatography. The notable exception is the omission of the 2,5-ADP affinity resin step to avoid the unusual biphasic binding isotherms during ITC experiment.
Name:
FAD-Binding Domain
Synonyms:
residue 273 to 492 of NADPH--cytochrome P450 reductase | NCPR_HUMAN | POR | CYPOR
Type:
enzyme co-factor binding domain
Mol. Mass.:
24688.74
Organism:
Human
Description:
P16435[273-492]
Residue:
220
Sequence:
PPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNW
  
Syringe React
Source:
Sigma-Aldrich
Name:
BDBM11941
Synonyms:
{[(2R,3R,4R,5R)-5-(6-amino-9H-purin-9-yl)-3-hydroxy-4-(phosphonooxy)oxolan-2-yl]methoxy}phosphonic acid | ADENOSINE-2 -5 -DIPHOSPHATE | 2,5-ADP
Type:
Nucleoside or nucleotide
Emp. Form.:
TBD
Mol. Mass.:
TBD
SMILES:
TBD
Structure:
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