Tuning reduction potentials of type 1 copper center in azurin by replacing a histidine ligand with its isostructural analogues

Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine. While the cysteine and methionine in azurin have been replaced with their respective isostructural analogues of unnatural amino acids to rev...

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Published inJournal of inorganic biochemistry Vol. 234; p. 111863
Main Authors Yu, Yang, Marshall, Nicholas M., Garner, Dewain K., Nilges, Mark J., Lu, Yi
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.09.2022
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Abstract Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine. While the cysteine and methionine in azurin have been replaced with their respective isostructural analogues of unnatural amino acids to reveal their roles in tuning electronic structures and functional properties, such as reduction potentials (E°′), the histidine ligands have not been probed in this way. We herein report the substitution of His117 in azurin with three unnatural isostructural analogues, 5-nitrohistidine(Ntr), thiazolylalanine(SHis) and 1-methylhistidine(MeH) by expressed protein ligation. While UV–vis absorption and electron paramagnetic resonance spectroscopies confirm that isostructural replacement results in minimal structural change in the Cu(II) state, the E°′ of these variants increases with increasing pKa of the δ nitrogens of the imidazole. This counter-intuitive relationship between E°′ of the protein and pKa of the sidechain group suggests additional factors may play a role in tuning E°′. Replacing His117 in azurin with three isostructural analogues, 5-nitrohistidine(Ntr), thiazolylalanine(SHis) and 1-methylhistidine(MeH) resulted in linear tuning of reduction potentials of the type 1 Cu2+/Cu+ couple. [Display omitted] •The histidine ligand in azurin is probed with its unnatural amino acid analogs.•Minimal structural perturbation was observed by spectroscopic studies.•Redox potentials of the variants increase with increasing pKa's of the histidine analogs.•The correlation between redox potentials and pKa's of the histidines is counter-intuitive.•This finding suggests additional factors may play a role in tuning the redox potentials.
AbstractList Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine. While the cysteine and methionine in azurin have been replaced with their respective isostructural analogues of unnatural amino acids to reveal their roles in tuning electronic structures and functional properties, such as reduction potentials (E°'), the histidine ligands have not been probed in this way. We herein report the substitution of His117 in azurin with three unnatural isostructural analogues, 5-nitrohistidine(Ntr), thiazolylalanine(SHis) and 1-methylhistidine(MeH) by expressed protein ligation. While UV-vis absorption and electron paramagnetic resonance spectroscopies confirm that isostructural replacement results in minimal structural change in the Cu(II) state, the E°' of these variants increases with increasing pKa of the δ nitrogens of the imidazole. This counter-intuitive relationship between E°' of the protein and pKa of the sidechain group suggests additional factors may play a role in tuning E°'.
Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine. While the cysteine and methionine in azurin have been replaced with their respective isostructural analogues of unnatural amino acids to reveal their roles in tuning electronic structures and functional properties, such as reduction potentials (E°′), the histidine ligands have not been probed in this way. We herein report the substitution of His117 in azurin with three unnatural isostructural analogues, 5-nitrohistidine(Ntr), thiazolylalanine(SHis) and 1-methylhistidine(MeH) by expressed protein ligation. While UV–vis absorption and electron paramagnetic resonance spectroscopies confirm that isostructural replacement results in minimal structural change in the Cu(II) state, the E°′ of these variants increases with increasing pKa of the δ nitrogens of the imidazole. This counter-intuitive relationship between E°′ of the protein and pKa of the sidechain group suggests additional factors may play a role in tuning E°′. Replacing His117 in azurin with three isostructural analogues, 5-nitrohistidine(Ntr), thiazolylalanine(SHis) and 1-methylhistidine(MeH) resulted in linear tuning of reduction potentials of the type 1 Cu2+/Cu+ couple. [Display omitted] •The histidine ligand in azurin is probed with its unnatural amino acid analogs.•Minimal structural perturbation was observed by spectroscopic studies.•Redox potentials of the variants increase with increasing pKa's of the histidine analogs.•The correlation between redox potentials and pKa's of the histidines is counter-intuitive.•This finding suggests additional factors may play a role in tuning the redox potentials.
ArticleNumber 111863
Author Marshall, Nicholas M.
Lu, Yi
Yu, Yang
Garner, Dewain K.
Nilges, Mark J.
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Keywords Redox
Blue copper
Electron transfer
Protein engineering
Cupredoxins
Unnatural amino acids
Language English
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Snippet Type 1 copper proteins have a conserved ligand set of one cysteine and two histidines, with many proteins, such as azurin, also containing an axial methionine....
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SubjectTerms Blue copper
Cupredoxins
Electron transfer
Protein engineering
Redox
Unnatural amino acids
Title Tuning reduction potentials of type 1 copper center in azurin by replacing a histidine ligand with its isostructural analogues
URI https://dx.doi.org/10.1016/j.jinorgbio.2022.111863
https://www.ncbi.nlm.nih.gov/pubmed/35691263
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