Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.

Scientific reports - 25 Feb 2016

Colthart Allison M, Tietz Drew R, Ni Yuhua, Friedman Jessica L, Dang Marina, Pochapsky Thomas C

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytochrome P-450 Enzyme System

Share to Models, Molecular

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 26911901
DOI: 10.1038/srep22035
PMCID: PMC4766564

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.PMID 26911901Read ↗

Some Surprising Implications of NMR-directed Simulations of Substrate Recognition and Binding by Cytochrome P450cam (CYP101A1).Semantic proximity Read ↗

Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1).Semantic proximity Read ↗

The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM.Semantic proximity Read ↗

Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam.Semantic proximity Read ↗

Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.Semantic proximity Read ↗

I helix Mediates the Allosteric Regulation in Cytochrome P450camSemantic proximity Read ↗

Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant.Semantic proximity Read ↗

Investigation of the low frequency dynamics of heme proteins: native and mutant cytochrome P450(cam) and redox partner complexes.Semantic proximity Read ↗

Stabilization and spectroscopic characterization of the dioxygen complex of wild-type cytochrome P4502B4 (CYP2B4) and its distal side E301Q, T302A and proximal side F429H mutants at subzero temperatures.Semantic proximity Read ↗

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.Semantic proximity Read ↗

L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors.Semantic proximity Read ↗

Hidden alternative structures of proline isomerase essential for catalysis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.