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

Molecular dynamics simulations indicate that F87W,T185F-cytochrome P450cam may reductively dehalogenate 1,1,1-trichloroethane.

Journal of biomolecular structure & dynamics - 1 Dec 1995

Manchester J I, Ornstein R L

Abstract excerpt

Cytochrome P450cam is capable of reductively dehalogenating several chlorinated alkanes at low, but measurable, rates. In previous investigations of structure-function relationships in this enzyme using molecular dynamics simulations, we noticed that 1,1,1-trichloroethane (TCA) exhibits a very high degree of mobility in the active site due to its smaller molecular volume relative to the native substrate,...

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 Computer Simulation
Share to Cytochrome P-450 Enzyme System

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

Share to Models, Molecular

Share to Mutation

Share to Oxidation-Reduction

Share to Structure-Activity Relationship

Share to Substrate Specificity

Source

Identifiers

PMID: 8825721
DOI: 10.1080/07391102.1995.10508851

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular dynamics simulations indicate that F87W,T185F-cytochrome P450cam may reductively dehalogenate 1,1,1-trichloroethane.PMID 8825721Read ↗

Mechanism of enhanced conversion of 1,2,3-trichloropropane by mutant haloalkane dehalogenase revealed by molecular modeling.Semantic proximity Read ↗

Exceptionally stable salt bridges in cytochrome P450cam have functional roles.Semantic proximity Read ↗

Catalytic Cycle of Haloalkane Dehalogenases Toward Unnatural Substrates Explored by Computational Modeling.Semantic proximity Read ↗

Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy.Semantic proximity Read ↗

Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.Semantic proximity Read ↗

A trade-off between catalytic power and substrate inhibition in TCHQ dehalogenase.Semantic proximity Read ↗

Structure-activity correlations in pentachlorobenzene oxidation by engineered cytochrome P450cam.Semantic proximity Read ↗

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

Structural and functional characterization of "laboratory evolved" cytochrome P450cam mutants showing enhanced naphthalene oxygenation activity.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 ↗

Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants.Semantic proximity Read ↗

Redox control of the P450cam catalytic cycle: effects of Y96F active site mutation and binding of a non-natural substrate.Semantic proximity Read ↗

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