PH-Induced Binding of the Axial Ligand in an Engineered CuA Site Favors the πu State

Marcos N. Morgada; Florencia Emiliani; Kelly N. Chacón; Damián Álvarez-Paggi; Daniel H. Murgida; Ninian J. Blackburn; Luciano A. Abriata; Alejandro J. Vila

doi:10.1021/acs.inorgchem.9b01868

PH-Induced Binding of the Axial Ligand in an Engineered Cu_A Site Favors the π_u State

Marcos N. Morgada, Florencia Emiliani, Kelly N. Chacón, Damián Álvarez-Paggi, Daniel H. Murgida, Ninian J. Blackburn, Luciano A. Abriata, Alejandro J. Vila

Chemical Physiology and Biochemistry

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

Abstract

Cu_A centers perform efficient long-range electron transfer. The electronic structure of native Cu_A sites can be described by a double-potential well with a dominant σ_u∗ ground state in fast equilibrium with a less populated π_u ground state. Here, we report a Cu_A mutant in which a lysine was introduced in the axial position. This results in a highly unstable protein with a pH-dependent population of the two ground states. Deep analysis of the high-pH form of this variant shows the stabilization of the π_u ground state due to direct binding of the Lys residue to the copper center that we attribute to deprotonation of this residue.

Original language	English (US)
Pages (from-to)	15687-15691
Number of pages	5
Journal	Inorganic Chemistry
Volume	58
Issue number	23
DOIs	https://doi.org/10.1021/acs.inorgchem.9b01868
State	Published - Dec 2 2019

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry

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10.1021/acs.inorgchem.9b01868

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title = "PH-Induced Binding of the Axial Ligand in an Engineered CuA Site Favors the πu State",

abstract = "CuA centers perform efficient long-range electron transfer. The electronic structure of native CuA sites can be described by a double-potential well with a dominant σu∗ ground state in fast equilibrium with a less populated πu ground state. Here, we report a CuA mutant in which a lysine was introduced in the axial position. This results in a highly unstable protein with a pH-dependent population of the two ground states. Deep analysis of the high-pH form of this variant shows the stabilization of the πu ground state due to direct binding of the Lys residue to the copper center that we attribute to deprotonation of this residue.",

author = "Morgada, {Marcos N.} and Florencia Emiliani and Chac{\'o}n, {Kelly N.} and Dami{\'a}n {\'A}lvarez-Paggi and Murgida, {Daniel H.} and Blackburn, {Ninian J.} and Abriata, {Luciano A.} and Vila, {Alejandro J.}",

note = "Publisher Copyright: Copyright {\textcopyright} 2019 American Chemical Society.",

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doi = "10.1021/acs.inorgchem.9b01868",

language = "English (US)",

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T1 - PH-Induced Binding of the Axial Ligand in an Engineered CuA Site Favors the πu State

AU - Morgada, Marcos N.

AU - Emiliani, Florencia

AU - Chacón, Kelly N.

AU - Álvarez-Paggi, Damián

AU - Murgida, Daniel H.

AU - Blackburn, Ninian J.

AU - Abriata, Luciano A.

AU - Vila, Alejandro J.

PY - 2019/12/2

Y1 - 2019/12/2

N2 - CuA centers perform efficient long-range electron transfer. The electronic structure of native CuA sites can be described by a double-potential well with a dominant σu∗ ground state in fast equilibrium with a less populated πu ground state. Here, we report a CuA mutant in which a lysine was introduced in the axial position. This results in a highly unstable protein with a pH-dependent population of the two ground states. Deep analysis of the high-pH form of this variant shows the stabilization of the πu ground state due to direct binding of the Lys residue to the copper center that we attribute to deprotonation of this residue.

AB - CuA centers perform efficient long-range electron transfer. The electronic structure of native CuA sites can be described by a double-potential well with a dominant σu∗ ground state in fast equilibrium with a less populated πu ground state. Here, we report a CuA mutant in which a lysine was introduced in the axial position. This results in a highly unstable protein with a pH-dependent population of the two ground states. Deep analysis of the high-pH form of this variant shows the stabilization of the πu ground state due to direct binding of the Lys residue to the copper center that we attribute to deprotonation of this residue.

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JO - Inorganic Chemistry

JF - Inorganic Chemistry

IS - 23

ER -

PH-Induced Binding of the Axial Ligand in an Engineered Cu_A Site Favors the π_u State

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