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Predicted structure and possible ionmotive mechanism of the sodium‐linked NADH‐ubiquinone oxidoreductase of Vibrio alginolyticus
Author(s) -
Rich Peter R.,
Meunier Brigitte,
Ward F.Bruce
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01164-a
Subject(s) - oxidoreductase , ferredoxin , cofactor , nad+ kinase , operon , biochemistry , vibrio alginolyticus , enzyme , biology , nadh dehydrogenase , chemistry , stereochemistry , protein subunit , vibrio , gene , bacteria , genetics , escherichia coli
Two groups have now published sequences of the six genes contained in the operon coding for the sodium‐linked NADH‐ubiquinone oxidoreductase of Vibrio alginolyticus . Sequence analyses indicate that this enzyme is unrelated to other known respiratory NADH dehydrogenases. A search for cofactor motifs suggests that the enzyme contains only one FAD, a ferredoxin‐type iron sulphur centre, and the NADH‐binding site. These are all located on NqrF, a subunit that can be recognized as a new member of a large diverse family of NAD(P)H‐oxidizing flavoenzymes. A possible model of ion‐coupling is presented, based upon this new information.