The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin.

Abstract:

:M98Q amicyanin is isolated with zinc bound to its type 1 copper-binding site. The influence of the axial ligand of the type 1 copper site on metal specificity is strongest prior to the completion of protein folding and adoption of the final type 1 site geometry. The preference for zinc over copper correlated with the selectivity of apoamicyanin in vitro in the partially folded, rather than the completely folded state. These results suggest that metal incorporation in vivo occurs during protein folding in the periplasm and not to a preformed type 1 site.

journal_name

J Inorg Biochem

authors

Ma JK,Lee S,Choi M,Bishop GR,Hosler JP,Davidson VL

doi

10.1016/j.jinorgbio.2007.09.007

subject

Has Abstract

pub_date

2008-02-01 00:00:00

pages

342-6

issue

2

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(07)00265-6

journal_volume

102

pub_type

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