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

John K. Ma; Sheeyong Lee; Moonsung Choi; G. Reid Bishop; Jonathan P. Hosler; Victor L. Davidson

doi:10.1016/j.jinorgbio.2007.09.007

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

John K. Ma, Sheeyong Lee, Moonsung Choi, G. Reid Bishop, Jonathan P. Hosler, Victor L. Davidson

Dept. of Optometry

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

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.

Original language	English
Pages (from-to)	342-346
Number of pages	5
Journal	Journal of Inorganic Biochemistry
Volume	102
Issue number	2
DOIs	https://doi.org/10.1016/j.jinorgbio.2007.09.007
State	Published - Feb 2008

Keywords

Azurin
Cupredoxin
Metalloprotein assembly
Redox protein

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10.1016/j.jinorgbio.2007.09.007

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title = "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.",

keywords = "Azurin, Cupredoxin, Metalloprotein assembly, Redox protein",

author = "Ma, \{John K.\} and Sheeyong Lee and Moonsung Choi and Bishop, \{G. Reid\} and Hosler, \{Jonathan P.\} and Davidson, \{Victor L.\}",

year = "2008",

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doi = "10.1016/j.jinorgbio.2007.09.007",

language = "English",

volume = "102",

pages = "342--346",

journal = "Journal of Inorganic Biochemistry",

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T1 - The axial ligand and extent of protein folding determine whether Zn or Cu binds to amicyanin

AU - Ma, John K.

AU - Lee, Sheeyong

AU - Choi, Moonsung

AU - Bishop, G. Reid

AU - Hosler, Jonathan P.

AU - Davidson, Victor L.

PY - 2008/2

Y1 - 2008/2

N2 - 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.

AB - 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.

KW - Azurin

KW - Cupredoxin

KW - Metalloprotein assembly

KW - Redox protein

UR - http://www.scopus.com/inward/record.url?scp=38149134599&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2007.09.007

DO - 10.1016/j.jinorgbio.2007.09.007

M3 - Article

C2 - 17986390

AN - SCOPUS:38149134599

SN - 0162-0134

VL - 102

SP - 342

EP - 346

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

IS - 2

ER -

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

Abstract

Keywords

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