A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.
about
Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.The Hinge Segment of Human NADPH-Cytochrome P450 Reductase in Conformational Switching: The Critical Role of Ionic Strength.Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strength
P2860
A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
A well-balanced preexisting eq ...... ultidomain diflavin reductase.
@en
type
label
A well-balanced preexisting eq ...... ultidomain diflavin reductase.
@en
prefLabel
A well-balanced preexisting eq ...... ultidomain diflavin reductase.
@en
P2093
P2860
P50
P1433
P1476
A well-balanced preexisting eq ...... multidomain diflavin reductase
@en
P2093
Denis Pompon
Eric Guittet
Fataneh Fatemi
Javier Pérez
Oriane Frances
P2860
P304
P356
10.1016/J.BPJ.2015.01.032
P407
P577
2015-03-01T00:00:00Z