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

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.

Biochemistry - 13 Nov 2001

Ost T W, Miles C S, Munro A W, Murdoch J, Reid G A, Chapman S K

Abstract excerpt

Site-directed mutants of the phylogenetically conserved phenylalanine residue F393 were constructed in flavocytochrome P450 BM3 from Bacillus megaterium. The high degree of conservation of this residue in the P450 superfamily and its proximity to the heme (and its ligand Cys400) infers an essential role in P450 activity. Extensive kinetic and thermodynamic characterization of mutant enzymes F393A, F393H, and...

Read the complete abstract on PubMed

Topics

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

Share to Carbon Monoxide
Share to Heme
Share to Mixed Function Oxygenases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NADPH-Ferrihemoprotein Reductase

Share to Oxygen

Share to Phenylalanine

Share to Sulfur

Share to Titrimetry

Source

Identifiers

PMID: 11695888
DOI: 10.1021/bi010716m

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

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.PMID 11695888Read ↗

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.Semantic proximity Read ↗

Novel haem co-ordination variants of flavocytochrome P450BM3.Semantic proximity Read ↗

Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.Semantic proximity Read ↗

Key mutations alter the cytochrome P450 BM3 conformational landscape and remove inherent substrate bias.Semantic proximity Read ↗

Flavocytochrome P450 BM3 mutant A264E undergoes substrate-dependent formation of a novel heme iron ligand set.Semantic proximity Read ↗

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.Semantic proximity Read ↗

Switching pyridine nucleotide specificity in P450 BM3: mechanistic analysis of the W1046H and W1046A enzymes.Semantic proximity Read ↗

Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450BM3 Variants.Semantic proximity Read ↗

The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3.Semantic proximity Read ↗

Thr268 in substrate binding and catalysis in P450BM-3.Semantic proximity Read ↗

P450(BM3) (CYP102A1): connecting the dots.Semantic proximity Read ↗

Laboratory evolution of P450 BM3 for mediated electron transfer yielding an activity-improved and reductase-independent variant.Semantic proximity Read ↗

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