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Related Concept Videos

Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Globular and Fibrous Proteins

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Protein and Protein Structure02:15

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Protein Dynamics in Living Cells01:19

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Protein Organization01:24

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Related Experiment Video

Updated: Jul 5, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

Structural studies on flavodiiron proteins.

João B Vicente1, Maria Arménia Carrondo, Miguel Teixeira

  • 1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.

Methods in Enzymology
|April 25, 2008
PubMed
Summary
This summary is machine-generated.

Flavodiiron proteins (FDPs) possess distinct N-terminal and C-terminal domains crucial for NO and O2 reduction. Structural insights into FDPs are advancing, but further studies are needed to fully understand their substrate activation mechanisms.

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Last Updated: Jul 5, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Flavodiiron proteins (FDPs) are a conserved protein family with a core structure of approximately 400 residues.
  • FDPs contain two distinct structural domains: an N-terminal metallo-beta-lactamase-like domain and a C-terminal flavodoxin-like domain.

Purpose of the Study:

  • To elucidate the structural basis of flavodiiron protein function.
  • To investigate the active site and substrate binding mechanisms of FDPs.

Main Methods:

  • Crystallographic studies were employed to determine the structures of FDPs.
  • Analysis of protein domains, active sites, and ligand interactions.

Main Results:

  • The N-terminal domain features a nonheme diiron center with carboxylate and histidine ligands, acting as the active site for NO and/or O2 reduction.
  • The C-terminal domain contains a flavin mononucleotide (FMN) moiety stabilized by non-covalent interactions.
  • Structural variations were observed, particularly at the diiron site, across different conditions and oxidation states.

Conclusions:

  • FDPs exhibit a conserved structural architecture with specialized domains for redox activity.
  • Current structural data provide partial understanding of FDPs but do not fully resolve substrate activation mechanisms.
  • Further crystallographic investigations are necessary to gain deeper insights into FDP function and substrate specificity.