A novel vanadium reductase, Vanabin2, forms a possible cascade involved in electron transfer.
The unusual ascidian ability to accumulate high levels of vanadium ions at concentrations of up to 350 mM, a 10(7)-fold increase over that found in seawater, has been attracting interdisciplinary attention for a century. Accumulated V(V) is finally reduced to V(III) via V(IV) in ascidian vanadocytes. Reducing agents must therefore participate in the reduction. Previously, we identified a vanadium-binding protein, Vanabin2, in which all 18 cysteines form nine disulfide bonds. Here, we report that Vanabin2 is a novel vanadium reductase because partial cleavage of its disulfide bonds results in the reduction of V(V) to V(IV). We propose that Vanabin2 forms a possible electron transfer cascade from the electron donor, NADPH, via glutathione reductase, glutathione, and Vanabin2 to the acceptor, and vanadium ions conjugated through thiol-disulfide exchange reactions.
Kawakami
Norifumi
N
Department of Biological Science, Graduate School of Science, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8526, Japan.
Ueki
Tatsuya
T
Amata
Yusuke
Y
Kanamori
Kan
K
Matsuo
Koichi
K
Gekko
Kunihiko
K
Michibata
Hitoshi
H