Characterization of VDAC1 as a plasma membrane NADH-oxidoreductase

Mark A Baker, Jennifer Dung Ly Huynh, Alfons Lawen

Research output: Contribution to journalArticleResearchpeer-review

18 Citations (Scopus)

Abstract

We have recently demonstrated that voltage dependent anion selective channel 1 (porin, isoform 1) can function as a transplasma membrane NADH:ferricyanide-reductase. However, both the specific redox characteristics and the mechanism of electron transport in this enzyme presently remain unclear. Here we demonstrate that the redox capability of porin 1 is specific for ferricyanide as this same enzyme cannot reduce DCIP or cytochrome c in vitro. Furthermore, NADH-dependent ferricyanide reduction associated with VDAC1 is not sensitive to the anion channel inhibitors DIDS and dextran sulfate. However, this activity can be inhibited by thiol chelators, suggesting that at least one of the two cysteine groups present in VDAC1 are critical for electron transfer. We propose a model on how electron transport may occur in VDAC1.
Original languageEnglish
Pages (from-to)215 - 221
Number of pages7
JournalBioFactors
Volume21
Issue number1-4
Publication statusPublished - 2004

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