L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.
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P450cam Visits an Open Conformation in the Absence of Substrate ,Synergistic Effects of Mutations in Cytochrome P450cam Designed To Mimic CYP101D1The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilisInvestigation of the low frequency dynamics of heme proteins: native and mutant cytochrome P450(cam) and redox partner complexesHeme enzyme structure and function.Electron transfer between cytochrome P450cin and its FMN-containing redox partner, cindoxin.Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxinPutidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis.Structural biology of p450-oxy complexes.Conformational plasticity and structure/function relationships in cytochromes P450.Structural biology of redox partner interactions in P450cam monooxygenase: a fresh look at an old system.Oxygen activation and redox partner binding in cytochromes P450.Identification of productive and futile encounters in an electron transfer protein complex.Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity.Solution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation.A functional proline switch in cytochrome P450cam.Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam.Combined QM/MM calculations of active-site vibrations in binding process of P450cam to putidaredoxin.Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P-450-CAM: probing the effector role of putidaredoxin in catalysis.Interaction between substrate and oxygen ligand responsible for effective O-O bond cleavage in bovine cytochrome P450 steroid 21-hydroxylase proved by Raman spectroscopy.
P2860
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P2860
L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.
description
2004 nî lūn-bûn
@nan
2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
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2004年學術文章
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name
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@en
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@nl
type
label
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@en
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@nl
prefLabel
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@en
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@nl
P2093
P2860
P356
P1476
L358P mutation on cytochrome P ...... -P450cam from electron donors.
@en
P2093
Isao Morishima
Koichiro Ishimori
Shiro Yoshioka
Takehiko Tosha
P2860
P304
42836-42843
P356
10.1074/JBC.M404216200
P407
P577
2004-07-21T00:00:00Z