ArticleScientific reports2016
Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Bacterial Transformation of Adamantane and Its Derivatives: Regioselectivity and Biocatalytic Approaches.Biology · 2025Review
- Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2.Journal of inorganic biochemistry · 2023Article
- Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450Biochemistry · 2022Article
- Computer-Aided (In Silico) Modeling of Cytochrome P450-Mediated Food-Drug Interactions (FDI).International journal of molecular sciences · 2022Review
- Updating the Paradigm: Redox Partner Binding and Conformational Dynamics in Cytochromes P450.Accounts of chemical research · 2022Review
- A cytochrome P450 CYP81AM1 from Tripterygium wilfordii catalyses the C-15 hydroxylation of dehydroabietic acid.Planta · 2021Article
- Partial Opening of Cytochrome P450cam (CYP101A1) Is Driven by Allostery and Putidaredoxin Binding.Biochemistry · 2021Article
- A dynamic understanding of cytochrome P450 structure and function through solution NMR.Current opinion in biotechnology · 2021Review
- Reconciling conformational heterogeneity and substrate recognition in cytochrome P450.Biophysical journal · 2021Article
- Dynamics underlying hydroxylation selectivity of cytochrome P450cam.Biophysical journal · 2021Article
- Linkage between Proximal and Distal Movements of P450cam Induced by Putidaredoxin.Biochemistry · 2020Article
- Heterologous coexpression of the benzoate-para-hydroxylase CYP53B1 with different cytochrome P450 reductases in various yeasts.Microbial biotechnology · 2019Article
- Human cytochrome P450 enzymes bind drugs and other substrates mainly through conformational-selection modes.The Journal of biological chemistry · 2019Article
- What Your Crystal Structure Will Not Tell You about Enzyme Function.Accounts of chemical research · 2019Article
- Lipid composition and macromolecular crowding effects on CYP2J2-mediated drug metabolism in nanodiscs.Protein science : a publication of the Protein Society · 2019Article
- Ligand and Redox Partner Binding Generates a New Conformational State in Cytochrome P450cam (CYP101A1).Journal of the American Chemical Society · 2019Article
- Entropic contribution to enhanced thermal stability in the thermostable P450 CYP119.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Some Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450Journal of molecular biology · 2018Article
- Spectroscopic studies of the cytochrome P450 reaction mechanisms.Biochimica et biophysica acta. Proteins and proteomics · 2018Review
- NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450.Biochimica et biophysica acta. Proteins and proteomics · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Cytochrome P450 monooxygenases typically catalyze the insertion of one atom of oxygen from O2 into unactivated carbon-hydrogen and carbon-carbon bonds, with concomitant reduction of the other oxygen atom to H2O by NAD(P)H. Comparison of the average structures of the camphor hydroxylase cytochrome P450(cam) (CYP101) obtained from residual dipolar coupling (RDC)-restrained molecular dynamics (MD) in the presence and absence of substrate camphor shows structural displacements resulting from the essential collapse of the active site upon substrate removal. This collapse has conformational consequences that extend across the protein structure, none of which were observed in analogous crystallographic structures. Mutations were made to test the involvement of the observed conformational changes in substrate binding and recognition. All of the mutations performed based upon the NMR-detected perturbations, even those remote from the active site, resulted in modified substrate selectivity, enzyme efficiency and/or haem iron spin state. The results demonstrate that solution NMR can provide insights into enzyme structure-function relationships that are difficult to obtain by other methods.
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