The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion

Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbo...
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Autor*in:	Claire C. Mammoser [verfasserIn] Brynn E. LeMasters [verfasserIn] Sydney G. Edwards [verfasserIn] Emma M. McRae [verfasserIn] M. Hunter Mullins [verfasserIn] Yiqi Wang [verfasserIn] Nicholas M. Garcia [verfasserIn] Katherine A. Edmonds [verfasserIn] David P. Giedroc [verfasserIn] Megan C. Thielges [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Übergeordnetes Werk:	In: Communications Chemistry - Nature Portfolio, 2018, 6(2023), 1, Seite 9
Übergeordnetes Werk:	volume:6 ; year:2023 ; number:1 ; pages:9

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1038/s42004-023-00977-4

Katalog-ID:	DOAJ093302800

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allfields	10.1038/s42004-023-00977-4 doi (DE-627)DOAJ093302800 (DE-599)DOAJf73a1aa8abd44131a24ab020e3fde38c DE-627 ger DE-627 rakwb eng QD1-999 Claire C. Mammoser verfasserin aut The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbon deuterium (C-D) bonds used as vibrational probes afford nonperturbative, selective characterization of the key cysteine and methionine copper ligands in both redox states. The structural integrity of Nostoc plastocyanin was perturbed by disrupting potential hydrogen bonds between loops of the cupredoxin fold via mutagenesis (S9A, N33A, N34A), variably raising the midpoint potential. The C-D vibrations show little change to suggest substantial alteration to the Cu(II) coordination in the oxidized state or in the Cu(I) interaction with the cysteine ligand. They rather indicate, along with visible and NMR spectroscopy, that the methionine ligand distinctly interacts more strongly with the Cu(I) ion, in line with the increases in midpoint potential. Here we show that the protein structure determines the redox properties by restricting the interaction between the methionine ligand and Cu(I) in the reduced state. Chemistry Brynn E. LeMasters verfasserin aut Sydney G. Edwards verfasserin aut Emma M. McRae verfasserin aut M. Hunter Mullins verfasserin aut Yiqi Wang verfasserin aut Nicholas M. Garcia verfasserin aut Katherine A. Edmonds verfasserin aut David P. Giedroc verfasserin aut Megan C. Thielges verfasserin aut In Communications Chemistry Nature Portfolio, 2018 6(2023), 1, Seite 9 (DE-627)1022213962 23993669 nnns volume:6 year:2023 number:1 pages:9 https://doi.org/10.1038/s42004-023-00977-4 kostenfrei https://doaj.org/article/f73a1aa8abd44131a24ab020e3fde38c kostenfrei https://doi.org/10.1038/s42004-023-00977-4 kostenfrei https://doaj.org/toc/2399-3669 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2023 1 9
spelling	10.1038/s42004-023-00977-4 doi (DE-627)DOAJ093302800 (DE-599)DOAJf73a1aa8abd44131a24ab020e3fde38c DE-627 ger DE-627 rakwb eng QD1-999 Claire C. Mammoser verfasserin aut The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbon deuterium (C-D) bonds used as vibrational probes afford nonperturbative, selective characterization of the key cysteine and methionine copper ligands in both redox states. The structural integrity of Nostoc plastocyanin was perturbed by disrupting potential hydrogen bonds between loops of the cupredoxin fold via mutagenesis (S9A, N33A, N34A), variably raising the midpoint potential. The C-D vibrations show little change to suggest substantial alteration to the Cu(II) coordination in the oxidized state or in the Cu(I) interaction with the cysteine ligand. They rather indicate, along with visible and NMR spectroscopy, that the methionine ligand distinctly interacts more strongly with the Cu(I) ion, in line with the increases in midpoint potential. Here we show that the protein structure determines the redox properties by restricting the interaction between the methionine ligand and Cu(I) in the reduced state. Chemistry Brynn E. LeMasters verfasserin aut Sydney G. Edwards verfasserin aut Emma M. McRae verfasserin aut M. Hunter Mullins verfasserin aut Yiqi Wang verfasserin aut Nicholas M. Garcia verfasserin aut Katherine A. Edmonds verfasserin aut David P. Giedroc verfasserin aut Megan C. Thielges verfasserin aut In Communications Chemistry Nature Portfolio, 2018 6(2023), 1, Seite 9 (DE-627)1022213962 23993669 nnns volume:6 year:2023 number:1 pages:9 https://doi.org/10.1038/s42004-023-00977-4 kostenfrei https://doaj.org/article/f73a1aa8abd44131a24ab020e3fde38c kostenfrei https://doi.org/10.1038/s42004-023-00977-4 kostenfrei https://doaj.org/toc/2399-3669 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2023 1 9
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authorswithroles_txt_mv	Claire C. Mammoser @@aut@@ Brynn E. LeMasters @@aut@@ Sydney G. Edwards @@aut@@ Emma M. McRae @@aut@@ M. Hunter Mullins @@aut@@ Yiqi Wang @@aut@@ Nicholas M. Garcia @@aut@@ Katherine A. Edmonds @@aut@@ David P. Giedroc @@aut@@ Megan C. Thielges @@aut@@
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Mammoser</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="4"><subfield code="a">The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2023</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. 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callnumber-first	Q - Science
author	Claire C. Mammoser
spellingShingle	Claire C. Mammoser misc QD1-999 misc Chemistry The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
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topic_title	QD1-999 The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
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title	The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
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title_full	The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
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author_browse	Claire C. Mammoser Brynn E. LeMasters Sydney G. Edwards Emma M. McRae M. Hunter Mullins Yiqi Wang Nicholas M. Garcia Katherine A. Edmonds David P. Giedroc Megan C. Thielges
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title_sort	structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
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title_auth	The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
abstract	Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbon deuterium (C-D) bonds used as vibrational probes afford nonperturbative, selective characterization of the key cysteine and methionine copper ligands in both redox states. The structural integrity of Nostoc plastocyanin was perturbed by disrupting potential hydrogen bonds between loops of the cupredoxin fold via mutagenesis (S9A, N33A, N34A), variably raising the midpoint potential. The C-D vibrations show little change to suggest substantial alteration to the Cu(II) coordination in the oxidized state or in the Cu(I) interaction with the cysteine ligand. They rather indicate, along with visible and NMR spectroscopy, that the methionine ligand distinctly interacts more strongly with the Cu(I) ion, in line with the increases in midpoint potential. Here we show that the protein structure determines the redox properties by restricting the interaction between the methionine ligand and Cu(I) in the reduced state.
abstractGer	Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbon deuterium (C-D) bonds used as vibrational probes afford nonperturbative, selective characterization of the key cysteine and methionine copper ligands in both redox states. The structural integrity of Nostoc plastocyanin was perturbed by disrupting potential hydrogen bonds between loops of the cupredoxin fold via mutagenesis (S9A, N33A, N34A), variably raising the midpoint potential. The C-D vibrations show little change to suggest substantial alteration to the Cu(II) coordination in the oxidized state or in the Cu(I) interaction with the cysteine ligand. They rather indicate, along with visible and NMR spectroscopy, that the methionine ligand distinctly interacts more strongly with the Cu(I) ion, in line with the increases in midpoint potential. Here we show that the protein structure determines the redox properties by restricting the interaction between the methionine ligand and Cu(I) in the reduced state.
abstract_unstemmed	Abstract Blue copper proteins are models for illustrating how proteins tune metal properties. Nevertheless, the mechanisms by which the protein controls the metal site remain to be fully elucidated. A hindrance is that the closed shell Cu(I) site is inaccessible to most spectroscopic analyses. Carbon deuterium (C-D) bonds used as vibrational probes afford nonperturbative, selective characterization of the key cysteine and methionine copper ligands in both redox states. The structural integrity of Nostoc plastocyanin was perturbed by disrupting potential hydrogen bonds between loops of the cupredoxin fold via mutagenesis (S9A, N33A, N34A), variably raising the midpoint potential. The C-D vibrations show little change to suggest substantial alteration to the Cu(II) coordination in the oxidized state or in the Cu(I) interaction with the cysteine ligand. They rather indicate, along with visible and NMR spectroscopy, that the methionine ligand distinctly interacts more strongly with the Cu(I) ion, in line with the increases in midpoint potential. Here we show that the protein structure determines the redox properties by restricting the interaction between the methionine ligand and Cu(I) in the reduced state.
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title_short	The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion
url	https://doi.org/10.1038/s42004-023-00977-4 https://doaj.org/article/f73a1aa8abd44131a24ab020e3fde38c https://doaj.org/toc/2399-3669
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The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion

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