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Characterization of VDAC1 as a plasma membrane NADH‐oxidoreductase
Author(s) -
Baker Mark A.,
Ly Jennifer D.,
Lawen Alfons
Publication year - 2004
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.552210143
Subject(s) - vdac1 , voltage dependent anion channel , chemistry , ferricyanide , redox , dids , biochemistry , electron transfer , electron transport chain , cytochrome c , membrane , mitochondrion , bacterial outer membrane , inorganic chemistry , photochemistry , escherichia coli , gene
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.