Journal article
Chromophore function and interaction in Escherichia coli DNA photolyase: Reconstitution of the apoenzyme with pterin and/or flavin derivatives
Biochemistry (Easton), v 29(2), pp 552-561
01 Jan 1990
PMID: 2405908
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Native DNA photolyase, as isolated from Escherichia coli , contains a neutral flavin radical (FADH) plus a pterin chromophore (5,10-methenyltetrahydropteroyl-polyglutamate) and can be converted to its physiologically significant form by reduction of FADH to fully reduced flavin (FADH sub(2)) with dithionite or by photoreduction. Various enzyme forms (EFAD sub(ox), EFADH, EFADH sub(2), EPteFAD sub(ox), EPteFADH, EPteFADH sub(2), EPte) containing stoichiometric amounts of FAD in either of its three oxidation states and/or 5,10-methenyltetrahydrofolate (Pte) have been prepared in reconstitution experiments. Studies with EFAD sub(ox) and EPte showed that these could be these preparations retained the ability to bind the missing chromophore. The results suggest that there could be considerable flexibility in the biological assembly of holoenzyme since the order of binding of the enzyme's chromophores is apparently unimportant, the binding of FAD is unaffected by its redox state, and enzyme preparations containing only one chromophore are reasonably stable.
Metrics
Details
- Title
- Chromophore function and interaction in Escherichia coli DNA photolyase: Reconstitution of the apoenzyme with pterin and/or flavin derivatives
- Creators
- M S Jorns - Hahnemann University HospitalBaoyu WangS JordanL Chanderkar
- Publication Details
- Biochemistry (Easton), v 29(2), pp 552-561
- Publisher
- American Chemical Society; Washington, DC
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1990CJ14100032
- Scopus ID
- 2-s2.0-0025100995
- Other Identifier
- 991019184304104721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology