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The P-type ATPase, CopB, of Enterococcus hirae is
required for the copper resistance displayed by this organism and thus
was postulated to be a copper pump. Using
Volume 270,
Number 16,
Issue of April 21, pp. 9217-9221, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Cu
and
Ag
, we here show ATP-driven
copper and silver accumulation catalyzed by CopB in native inside-out
membrane vesicles of E. hirae. CopB ATPase exhibited an
apparent K
for Cu
and
Ag
of 1 µ
M and for ATP of 10
µ
M. Transport was maximal at pH 6 and had an apparent
V
of 0.07
nmolmin
mg
for both
copper and silver transport. Vanadate displayed a biphasic effect on
transport: maximal inhibition was observed at 40 µ
M vanadate for copper transport and 60 µ
M for silver
transport, respectively. At higher vanadate concentrations, these
inhibitions were reversed. The CopB ATPase of E. hirae is thus
a pump for the extrusion of monovalent copper and silver ions, with
copper probably being the natural substrate.
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