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Published on: March 18, 2012

Excited flavin and pterin coenzyme molecules in evolution.

M S Kritsky1, T A Telegina, Y L Vechtomova

  • 1Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia. mkritsky@inbi.ras.ru

Biochemistry. Biokhimiia
|December 21, 2010
PubMed
Summary
This summary is machine-generated.

Flavin and pterin molecules convert light energy, but evolved into DNA repair and light sensing proteins, not bioenergy. These photoproteins, like DNA photolyases and cryptochromes, utilize excited flavins for distinct functions.

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Published on: August 14, 2019

Area of Science:

  • Biochemistry
  • Photochemistry
  • Evolutionary Biology

Background:

  • Flavin and pterin molecules are crucial for energy transfer and photocatalysis.
  • Prebiotic models show flavin pigments can convert light energy into ATP bonds.
  • Despite potential, excited flavins were not integrated into bioenergy systems during evolution.

Purpose of the Study:

  • To investigate the evolutionary trajectory of photochemical reactions involving flavins.
  • To understand the roles of flavin-excited molecules in DNA photolyases and light receptors.
  • To explore the structural and mechanistic differences among photoprotein families.

Main Methods:

  • Analysis of flavin and pterin molecule functions in energy transfer and photocatalysis.
  • Examination of photoprotein families (DNA photolyases, cryptochromes, LOV, BLUF domains).
  • Structural comparison of chromophore-binding domains and coenzyme properties.

Main Results:

  • Excited flavins are central to photochemical processes in DNA photolyases and cryptochromes.
  • Antenna molecules (MTHF, 8-HDF) supply excitation energy to reaction center flavins in some photolyases.
  • Structural divergence suggests independent evolutionary origins for photoprotein families.

Conclusions:

  • Photochemical reactions involving excited flavins evolved into specialized roles in DNA repair and light sensing.
  • Differences in chromophore-binding domains support the independent evolution of photoprotein families.
  • Specific coenzyme properties were likely key factors in their selection as chromophores.