Structural insights into functional properties of the oxidized form of cytochrome c oxidase

Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction inv...
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Autor*in:	Izumi Ishigami [verfasserIn] Raymond G. Sierra [verfasserIn] Zhen Su [verfasserIn] Ariana Peck [verfasserIn] Cong Wang [verfasserIn] Frederic Poitevin [verfasserIn] Stella Lisova [verfasserIn] Brandon Hayes [verfasserIn] Frank R. Moss [verfasserIn] Sébastien Boutet [verfasserIn] Robert E. Sublett [verfasserIn] Chun Hong Yoon [verfasserIn] Syun-Ru Yeh [verfasserIn] Denis L. Rousseau [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Übergeordnetes Werk:	In: Nature Communications - Nature Portfolio, 2016, 14(2023), 1, Seite 10
Übergeordnetes Werk:	volume:14 ; year:2023 ; number:1 ; pages:10

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1038/s41467-023-41533-x

Katalog-ID:	DOAJ092893503

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520			\|a Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO.
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allfields	10.1038/s41467-023-41533-x doi (DE-627)DOAJ092893503 (DE-599)DOAJ4cf0387559044a58973e6bfc59f08ca6 DE-627 ger DE-627 rakwb eng Izumi Ishigami verfasserin aut Structural insights into functional properties of the oxidized form of cytochrome c oxidase 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO. Science Q Raymond G. Sierra verfasserin aut Zhen Su verfasserin aut Ariana Peck verfasserin aut Cong Wang verfasserin aut Frederic Poitevin verfasserin aut Stella Lisova verfasserin aut Brandon Hayes verfasserin aut Frank R. Moss verfasserin aut Sébastien Boutet verfasserin aut Robert E. Sublett verfasserin aut Chun Hong Yoon verfasserin aut Syun-Ru Yeh verfasserin aut Denis L. Rousseau verfasserin aut In Nature Communications Nature Portfolio, 2016 14(2023), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:14 year:2023 number:1 pages:10 https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 kostenfrei https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 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_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2023 1 10
spelling	10.1038/s41467-023-41533-x doi (DE-627)DOAJ092893503 (DE-599)DOAJ4cf0387559044a58973e6bfc59f08ca6 DE-627 ger DE-627 rakwb eng Izumi Ishigami verfasserin aut Structural insights into functional properties of the oxidized form of cytochrome c oxidase 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO. Science Q Raymond G. Sierra verfasserin aut Zhen Su verfasserin aut Ariana Peck verfasserin aut Cong Wang verfasserin aut Frederic Poitevin verfasserin aut Stella Lisova verfasserin aut Brandon Hayes verfasserin aut Frank R. Moss verfasserin aut Sébastien Boutet verfasserin aut Robert E. Sublett verfasserin aut Chun Hong Yoon verfasserin aut Syun-Ru Yeh verfasserin aut Denis L. Rousseau verfasserin aut In Nature Communications Nature Portfolio, 2016 14(2023), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:14 year:2023 number:1 pages:10 https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 kostenfrei https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 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_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2023 1 10
allfields_unstemmed	10.1038/s41467-023-41533-x doi (DE-627)DOAJ092893503 (DE-599)DOAJ4cf0387559044a58973e6bfc59f08ca6 DE-627 ger DE-627 rakwb eng Izumi Ishigami verfasserin aut Structural insights into functional properties of the oxidized form of cytochrome c oxidase 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO. Science Q Raymond G. Sierra verfasserin aut Zhen Su verfasserin aut Ariana Peck verfasserin aut Cong Wang verfasserin aut Frederic Poitevin verfasserin aut Stella Lisova verfasserin aut Brandon Hayes verfasserin aut Frank R. Moss verfasserin aut Sébastien Boutet verfasserin aut Robert E. Sublett verfasserin aut Chun Hong Yoon verfasserin aut Syun-Ru Yeh verfasserin aut Denis L. Rousseau verfasserin aut In Nature Communications Nature Portfolio, 2016 14(2023), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:14 year:2023 number:1 pages:10 https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 kostenfrei https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 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_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2023 1 10
allfieldsGer	10.1038/s41467-023-41533-x doi (DE-627)DOAJ092893503 (DE-599)DOAJ4cf0387559044a58973e6bfc59f08ca6 DE-627 ger DE-627 rakwb eng Izumi Ishigami verfasserin aut Structural insights into functional properties of the oxidized form of cytochrome c oxidase 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO. Science Q Raymond G. Sierra verfasserin aut Zhen Su verfasserin aut Ariana Peck verfasserin aut Cong Wang verfasserin aut Frederic Poitevin verfasserin aut Stella Lisova verfasserin aut Brandon Hayes verfasserin aut Frank R. Moss verfasserin aut Sébastien Boutet verfasserin aut Robert E. Sublett verfasserin aut Chun Hong Yoon verfasserin aut Syun-Ru Yeh verfasserin aut Denis L. Rousseau verfasserin aut In Nature Communications Nature Portfolio, 2016 14(2023), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:14 year:2023 number:1 pages:10 https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 kostenfrei https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 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_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2023 1 10
allfieldsSound	10.1038/s41467-023-41533-x doi (DE-627)DOAJ092893503 (DE-599)DOAJ4cf0387559044a58973e6bfc59f08ca6 DE-627 ger DE-627 rakwb eng Izumi Ishigami verfasserin aut Structural insights into functional properties of the oxidized form of cytochrome c oxidase 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO. Science Q Raymond G. Sierra verfasserin aut Zhen Su verfasserin aut Ariana Peck verfasserin aut Cong Wang verfasserin aut Frederic Poitevin verfasserin aut Stella Lisova verfasserin aut Brandon Hayes verfasserin aut Frank R. Moss verfasserin aut Sébastien Boutet verfasserin aut Robert E. Sublett verfasserin aut Chun Hong Yoon verfasserin aut Syun-Ru Yeh verfasserin aut Denis L. Rousseau verfasserin aut In Nature Communications Nature Portfolio, 2016 14(2023), 1, Seite 10 (DE-627)626457688 (DE-600)2553671-0 20411723 nnns volume:14 year:2023 number:1 pages:10 https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 kostenfrei https://doi.org/10.1038/s41467-023-41533-x kostenfrei https://doaj.org/toc/2041-1723 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 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_171 GBV_ILN_211 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2110 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 14 2023 1 10
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spellingShingle	Izumi Ishigami misc Science misc Q Structural insights into functional properties of the oxidized form of cytochrome c oxidase
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title	Structural insights into functional properties of the oxidized form of cytochrome c oxidase
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author_browse	Izumi Ishigami Raymond G. Sierra Zhen Su Ariana Peck Cong Wang Frederic Poitevin Stella Lisova Brandon Hayes Frank R. Moss Sébastien Boutet Robert E. Sublett Chun Hong Yoon Syun-Ru Yeh Denis L. Rousseau
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title_sort	structural insights into functional properties of the oxidized form of cytochrome c oxidase
title_auth	Structural insights into functional properties of the oxidized form of cytochrome c oxidase
abstract	Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO.
abstractGer	Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO.
abstract_unstemmed	Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a 3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO.
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title_short	Structural insights into functional properties of the oxidized form of cytochrome c oxidase
url	https://doi.org/10.1038/s41467-023-41533-x https://doaj.org/article/4cf0387559044a58973e6bfc59f08ca6 https://doaj.org/toc/2041-1723
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Structural insights into functional properties of the oxidized form of cytochrome c oxidase

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