Redox-dependent dynamics in cytochrome P450cam
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Summary
The reduced enzyme exhibits lower-amplitude motions of secondary structural features than the oxidized enzyme on all of the time scales accessible to these experiments, and these differences are more pronounced in regions of the enzyme involved in substrate access to the active site and binding of putidaredoxin.
- Type
- article
- Published
- 2009-05-26
- Cited by
- 20
- References
- 26
- Access
- Open access
- OpenAlex
- https://openalex.org/W1963992020
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34882640
Keywords
Chemistry, Heme, Active site, Protein dynamics, Hemeprotein
References
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- The PyMOL Molecular Graphics System
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- A conserved histidine in vertebrate-type ferredoxins is critical for redox-dependent dynamics.
- Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.
- Redox‐dependent dynamics of putidaredoxin characterized by amide proton exchange
- Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR relaxation measurements.
- Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity.
- Essential role of the Arg112 residue of cytochrome P450cam for electron transfer from reduced putidaredoxin
- Protein dynamics measurements by TROSY-based NMR experiments.
- Investigation of oxidation state‐dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome C 553 by two‐dimensional 1H‐NMR spectra
- A structure-based model for cytochrome P450cam-putidaredoxin interactions.
- Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso‐1‐cytochrome c
- The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme.
- Nickel-specific response in the transcriptional regulator, Escherichia coli NikR.
- Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam.
- A functional proline switch in cytochrome P450cam.
- How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways.
- How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms.
Cited by
- Structural characterization of the Redox-Dependent differences in the Cytochrome P450cam-Putidaredoxin Complex using solution NMR spectroscopy
- Conformational Dynamics of Cytochrome P450cam Upon Ligand Binding
- Spectroscopic features of cytochrome P450 reaction intermediates
- Two-dimensional NMR and All-atom Molecular Dynamics of Cytochrome P450 CYP119 Reveal Hidden Conformational Substates*
- Functional characterization of cytochromes P450 2B from the desert woodrat Neotoma lepida
- Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444
- Three clusters of conformational states in P450cam reveal a multi-step pathway for closing of the substrate access channel,
- Redox State Dependence of Axial Ligand Dynamics in Nitrosomonas europaea Cytochrome c552
- Conformational Plasticity and Structure/Function Relationships in Cytochromes P450
- Solution Structural Ensembles of Substrate-Free Cytochrome P450cam,
- Plasticity of Cytochrome P450 2B4 as Investigated by Hydrogen-Deuterium Exchange Mass Spectrometry and X-ray Crystallography*
- Molecular Characterization of a Class I P450 Electron Transfer System from Novosphingobium aromaticivorans DSM12444*
- Role of Protein–Protein Interactions in Cytochrome P450-Mediated Drug Metabolism and Toxicity
- Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam,
- NANODISCS IN MEMBRANE BIOCHEMISTRY AND BIOPHYSICS
- Substrate recognition by two different P450s: Evidence for conserved roles in a common fold
- A large-scale comparative analysis of affinity, thermodynamics and functional characteristics of interactions of twelve cytochrome P450 isoforms and their redox partners.
- Combining small-molecule bioconjugation and hydrogen-deuterium exchange mass spectrometry (HDX-MS) to expose allostery: the case of human cytochrome P450 3A4
- Cymredoxin, a [2Fe-2S] ferredoxin, supports catalytic activity of the p-cymene oxidising P450 enzyme CYP108N12.
- Stereochemical Control of Redox CoII/CoIII-Cages with Switchable Cotton Effects Based on Labile-Static States.
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