ArticleEuropean biophysics journal : EBJ2013
Dihydrolipoic acid reduces cytochrome b561 proteins.
Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Spectral and Redox Properties of a Recombinant Mouse CytochromeMolecules (Basel, Switzerland) · 2023Article
- Comparison of insect and human cytochrome b561 proteins: Insights into candidate ferric reductases in insects.PloS one · 2023Article
- Duodenal cytochrome b (DCYTB) in iron metabolism: an update on function and regulation.Nutrients · 2015Review
- Cytochromes b561: ascorbate-mediated trans-membrane electron transport.Antioxidants & redox signaling · 2013Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome b561 (Cyt-b561) proteins constitute a family of trans-membrane proteins that are present in a wide variety of organisms. Two of their characteristic properties are the reducibility by ascorbate (ASC) and the presence of two distinct b-type hemes localized on two opposite sides of the membrane. Here we show that the tonoplast-localized and the putative tumor suppressor Cyt-b561 proteins can be reduced by other reductants than ASC and dithionite. A detailed spectral analysis of the ASC-dependent and dihydrolipoic acid (DHLA)-dependent reduction of these two Cyt-b561 proteins is also presented. Our results are discussed in relation to the known antioxidant capability of DHLA as well as its role in the regeneration of other antioxidant compounds of cells. These results allow us to speculate on new biological functions for the trans-membrane Cyt-b561 proteins.
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