A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase.
about
The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infectionStructural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxinCharacterization of Active Site Structure in CYP121: A CYTOCHROME P450 ESSENTIAL FOR VIABILITY OF MYCOBACTERIUM TUBERCULOSIS H37RvSubstrate binding induces structural changes in cytochrome P450camSite-Specific Incorporation of 3-Nitrotyrosine as a Probe of p K a Perturbation of Redox-Active Tyrosines in Ribonucleotide ReductaseStructure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzymeP450cin Active Site Water: Implications for Substrate Binding and Solvent AccessibilityStructure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE(CYP152L1) from theJeotgalicoccussp. 8456 BacteriumVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyProtein engineering of cytochrome p450(cam) (CYP101) for the oxidation of polycyclic aromatic hydrocarbonsInvestigation of the low frequency dynamics of heme proteins: native and mutant cytochrome P450(cam) and redox partner complexesRedox-dependent dynamics of putidaredoxin characterized by amide proton exchangeRedox potential control by drug binding to cytochrome P450 3A4Water oxidation by a cytochrome p450: mechanism and function of the reaction.Using resonance Raman cross-section data to estimate the spin state populations of Cytochromes P450.Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA.Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1. Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium.A direct electrode-driven P450 cycle for biocatalysis.Cytochrome P450 reductase: a harbinger of diffusible reduced oxygen speciesCytochrome P450 substrate specificities, substrate structural templates and enzyme active site geometries.Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450cam spin transition.Characterization of Cupriavidus metallidurans CYP116B1--a thiocarbamate herbicide oxygenating P450-phthalate dioxygenase reductase fusion protein.Allosteric phenomena in cytochrome P450-catalyzed monooxygenations.Identification of a functional water channel in cytochrome P450 enzymes.Chemical mechanisms for cytochrome P-450 oxidation: spectral and catalytic properties of a manganese-substituted protein.Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis.Stopped-Flow Studies of the Reduction of the Copper Centers Suggest a Bifurcated Electron Transfer Pathway in Peptidylglycine Monooxygenase.Oxygen activation by cytochrome P450 monooxygenaseSubstrate binding to cytochromes P450.Selenolate complexes of CYP101 and the heme-bound hHO-1/H25A proximal cavity mutantResonance Raman spectroscopy reveals that substrate structure selectively impacts the heme-bound diatomic ligands of CYP17.Methane-Oxidizing Enzymes: An Upstream Problem in Biological Gas-to-Liquids Conversion.The active site of the thermophilic CYP119 from Sulfolobus solfataricus.Mixing apples and oranges: Analysis of heterotropic cooperativity in cytochrome P450 3A4The study of enzyme mechanisms by a combination of cosolvent, low-temperature and high-pressure techniques.Cytochrome P-450 spin state: inorganic biochemistry of haem iron ligation and functional significance.Cytochromes P450: their active-site structure and mechanism of oxidation.A water-mediated allosteric network governs activation of Aurora kinase A.Electron tunneling through sensitizer wires bound to proteins.NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes.
P2860
Q24644351-F094AE2B-5F8F-490B-BD89-5FF3C3D82988Q24675963-9AD477D4-EDF2-4808-9A14-DB8506193214Q27652291-81B257A4-1A29-4CE5-BED6-698D06826854Q27653654-7E24C4AB-C29C-4231-A41E-9413C32F1A43Q27662095-3456E721-3E2D-4065-89A0-58BFD15D364BQ27677375-D67345EA-D4DF-4F54-A0D6-010FE96E4B5FQ27678939-7A55AFCD-8060-4B16-8270-59B787D61605Q27681396-1411AE8B-35DB-4233-83A2-97630161449CQ28304165-0CA81F4A-147F-41CF-BC78-058CEB8D368EQ28372807-0684DCFE-831D-4941-83BD-A26F9B9E2D05Q28740427-1C5F1F05-49A8-40DB-8A5B-1E9BEB2B9733Q28756229-C68B1ED8-CE84-4BFA-841F-070F5BDB273EQ28757148-69B4271E-BB4F-4499-AFDA-B8AEC47D0823Q30620700-CCA30FE4-42E9-448B-9F8D-B51E33B41E05Q30737738-4A1C0BCB-0E9A-431F-B98B-6CC74259EDC0Q31627018-07A63A52-F80D-49F3-85AF-6EB057A2C26CQ33286981-968AF2DE-6D29-4F33-85CC-065B1AC9FAABQ33710599-E6C84663-637D-4EAB-BE3A-1C1FF9C75E15Q33725593-75320737-6ADA-4ACC-86CE-E8E29C986F2AQ33856673-2A95B79D-F1CE-4823-B27A-DBE67D2607A3Q34129470-49EA25CD-419D-45CA-945E-5BD00DFB93D7Q34166732-2019D61B-F35F-4C41-819D-41938ADF9C5EQ34370833-3CDBF727-D7E2-47B5-B5C5-83E6C2D4DE47Q36032795-D4DF2A5D-BE42-4991-B634-CCF16E02BC85Q36313355-FBDF177C-C58B-46C7-A22E-D61301C9D152Q36871814-1D9BD88F-AB1E-4E2A-A3E4-7C778AB58E40Q36934070-881130AC-526E-4CBE-BF74-8F2686C7FC22Q37207087-017A5F70-42C3-4126-B515-F782209987D6Q37214645-022FA5C7-C712-449C-87B4-0908DA364FEEQ37305787-088A2491-AABA-467C-9098-AF1CE0D21F72Q37579896-E0D1D2BD-2604-4FAE-BDA8-3C28C04C4616Q37591825-8A5FA8F9-AE66-4B54-A244-DD880952C400Q38312581-2BE5AF10-D80D-43B8-B7A4-81390690D74FQ38393619-007ED6AE-18B4-42A8-851A-7C6D85DBF4DDQ39595006-A32B7973-5D51-4968-B98A-C103B20D9694Q40176481-90D1B7B4-E693-4975-ABD9-8356F5EDE67DQ40861918-0597FBF2-8402-400D-84D8-BA3031CEAAB4Q41654097-538C4983-1D82-4061-ABC4-7E4A87F8D704Q41948469-646575D9-0FF1-42F6-BC64-C30D309C187CQ42169217-FD68F635-F3AD-4A18-A5EB-DD257077131C
P2860
A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase.
description
1976 nî lūn-bûn
@nan
1976 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
name
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@ast
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@en
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@nl
type
label
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@ast
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@en
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@nl
prefLabel
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@ast
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@en
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@nl
P2860
P356
P1476
A thermodynamic model of regul ...... ibria in camphor monoxygenase.
@en
P2093
Gunsalus IC
P2860
P304
P356
10.1073/PNAS.73.4.1078
P407
P577
1976-04-01T00:00:00Z