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

Effector proteins from P450(cam) and methane monooxygenase: lessons in tuning nature's powerful reagents.

Biochemical and biophysical research communications - 5 Dec 2003

Brazeau Brian J, Wallar Bradley J, Lipscomb John D

Abstract excerpt

Effector proteins alter the kinetic or catalytic course of many oxygenase reactions. One of the first oxygenase effectors to be described was putidaredoxin, which serves to gate electron transfer into oxy-P450(cam). In the nonheme, methane monooxygenase (MMO) system, the B-component (MMOB) serves a distinct effector function by gating substrate and oxygen into the active site of the hydroxylase component (MMOH)....

Read the complete abstract on PubMed

Topics

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

Share to Coenzymes
Share to Computer Simulation
Share to Cross-Linking Reagents

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

Share to Electron-Transferring Flavoproteins

Share to Enzyme Activation

Share to Enzyme Stability

Share to Oxygenases

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 14630032
DOI: 10.1016/j.bbrc.2003.09.242

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

Effector proteins from P450(cam) and methane monooxygenase: lessons in tuning nature's powerful reagents.PMID 14630032Read ↗

Structural biology of redox partner interactions in P450cam monooxygenase: a fresh look at an old system.Semantic proximity Read ↗

Effector Roles of Putidaredoxin on Cytochrome P450cam Conformational States.Semantic proximity Read ↗

Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins.Semantic proximity Read ↗

Electron transport in cytochromes P-450 by covalent switching.Semantic proximity Read ↗

Residues in Methylosinus trichosporium OB3b methane monooxygenase component B involved in molecular interactions with reduced- and oxidized-hydroxylase component: a role for the N-terminus.Semantic proximity Read ↗

Tailoring an alien ferredoxin to support native-like P450 monooxygenase activity.Semantic proximity Read ↗

Arginines 65 and 310 in putidaredoxin reductase are critical for interaction with putidaredoxin.Semantic proximity Read ↗

Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling.Semantic proximity Read ↗

Proximal ligand control of heme iron coordination structure and reactivity with hydrogen peroxide: investigations of the myoglobin cavity mutant H93G with unnatural oxygen donor proximal ligands.Semantic proximity Read ↗

Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases.Semantic proximity Read ↗

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

Coenzyme binding during catalysis is beneficial for the stability of 4-hydroxyacetophenone monooxygenase.Semantic proximity Read ↗

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