The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.
about
Electron tunneling in protein crystalsMechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Heme enzyme structure and function.Uncovering the role of hydrophobic residues in cytochrome P450-cytochrome P450 reductase interactionsRate-limiting steps in cytochrome P450 catalysis.Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics studyThermal inactivation of the reductase domain of cytochrome P450 BM3.Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.An efficient light-driven P450 BM3 biocatalyst.Structural biology of redox partner interactions in P450cam monooxygenase: a fresh look at an old system.P450(BM3) (CYP102A1): connecting the dots.Redox properties of cytochrome p450BM3 measured by direct methods.
P2860
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P2860
The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
The FMN to heme electron trans ...... -heme domain interaction site.
@en
type
label
The FMN to heme electron trans ...... -heme domain interaction site.
@en
prefLabel
The FMN to heme electron trans ...... -heme domain interaction site.
@en
P2093
P2860
P356
P1476
The FMN to heme electron trans ...... -heme domain interaction site.
@en
P2093
Hazzard JT
Sevrioukova IF
P2860
P304
36097-36106
P356
10.1074/JBC.274.51.36097
P407
P577
1999-12-01T00:00:00Z