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

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

Archives of biochemistry and biophysics - 1 Mar 2011

Girvan Hazel M, Dunford Adrian J, Neeli Rajasekhar, Ekanem Idorenyin S, Waltham Timothy N, Joyce M Gordon, Leys David, Curtis Robin A, Williams Paul, Fisher Karl, Voice Michael W, Munro Andrew W

Abstract excerpt

Bacillus megaterium P450 BM3 (BM3) is a P450/P450 reductase fusion enzyme, where the dimer is considered the active form in NADPH-dependent fatty acid hydroxylation. The BM3 W1046A mutant was generated, removing an aromatic "shield" from its FAD isoalloxazine ring. W1046A BM3 is a catalytically active NADH-dependent lauric acid hydroxylase, with product formation slightly superior to the NADPH-driven enzyme. The...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus megaterium
Share to Electron Transport

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

Share to Flavin Mononucleotide

Share to Hydroxylation

Share to NADPH-Ferrihemoprotein Reductase

Share to Protein Multimerization

Source

Identifiers

PMID: 20868649
DOI: 10.1016/j.abb.2010.09.014

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

Flavocytochrome P450 BM3 mutant W1046A is a NADH-dependent fatty acid hydroxylase: implications for the mechanism of electron transfer in the P450 BM3 dimer.PMID 20868649Read ↗

The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase.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 ↗

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

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

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

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

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

Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3.Semantic proximity Read ↗

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

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

Structure, electronic properties and catalytic behaviour of an activity-enhancing CYP102A1 (P450(BM3)) variant.Semantic proximity Read ↗

Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.Semantic proximity Read ↗

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