Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Izumi Ishigami [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 114(2017), 30, Seite 8011 |
|---|---|
| Übergeordnetes Werk: |
volume:114 ; year:2017 ; number:30 ; pages:8011 |
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| 245 | 1 | 0 | |a Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature |
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| 520 | |a Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. | ||
| 650 | 4 | |a Artifacts | |
| 650 | 4 | |a Heme | |
| 650 | 4 | |a Unwinding | |
| 650 | 4 | |a Bioenergetics | |
| 650 | 4 | |a Mitochondria | |
| 650 | 4 | |a Cytochrome-c oxidase | |
| 650 | 4 | |a Electron transfer | |
| 650 | 4 | |a Carbon monoxide | |
| 650 | 4 | |a Radiation damage | |
| 650 | 4 | |a Radiation | |
| 650 | 4 | |a Allosteric properties | |
| 650 | 4 | |a Cobalt | |
| 650 | 4 | |a Crystal structure | |
| 650 | 4 | |a Crystallography | |
| 650 | 4 | |a Femtosecond | |
| 650 | 4 | |a pH effects | |
| 650 | 4 | |a Translocation | |
| 650 | 4 | |a Protons | |
| 650 | 4 | |a Temperature | |
| 650 | 4 | |a Free energy | |
| 650 | 4 | |a X-ray crystallography | |
| 650 | 4 | |a Structural damage | |
| 650 | 4 | |a Light sources | |
| 650 | 4 | |a Cytochrome | |
| 650 | 4 | |a Synchrotron radiation | |
| 650 | 4 | |a Atmospheric chemistry | |
| 650 | 4 | |a Oxidase | |
| 650 | 4 | |a Iron | |
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| 700 | 0 | |a Masahide Hikita |4 oth | |
| 700 | 0 | |a Chelsie E Conrad |4 oth | |
| 700 | 0 | |a Garrett Nelson |4 oth | |
| 700 | 0 | |a Jesse D Coe |4 oth | |
| 700 | 0 | |a Shibom Basu |4 oth | |
| 700 | 0 | |a Thomas D Grant |4 oth | |
| 700 | 0 | |a Matthew H Seaberg |4 oth | |
| 700 | 0 | |a Raymond G Sierra |4 oth | |
| 700 | 0 | |a Mark S Hunter |4 oth | |
| 700 | 0 | |a Petra Fromme |4 oth | |
| 700 | 0 | |a Raimund Fromme |4 oth | |
| 700 | 0 | |a Syun-Ru Yeh |4 oth | |
| 700 | 0 | |a Denis L Rousseau |4 oth | |
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PQ20171228 (DE-627)OLC1998531325 (DE-599)GBVOLC1998531325 (PRQ)p933-2bee6702a4a769bee1c2ce50897d37deb242eb4f4bb979e5c1bb06f721e3e6bf0 (KEY)0583363920170000114003008011crystalstructureofcoboundcytochromecoxidasedetermi DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Izumi Ishigami verfasserin aut Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. Artifacts Heme Unwinding Bioenergetics Mitochondria Cytochrome-c oxidase Electron transfer Carbon monoxide Radiation damage Radiation Allosteric properties Cobalt Crystal structure Crystallography Femtosecond pH effects Translocation Protons Temperature Free energy X-ray crystallography Structural damage Light sources Cytochrome Synchrotron radiation Atmospheric chemistry Oxidase Iron Nadia A Zatsepin oth Masahide Hikita oth Chelsie E Conrad oth Garrett Nelson oth Jesse D Coe oth Shibom Basu oth Thomas D Grant oth Matthew H Seaberg oth Raymond G Sierra oth Mark S Hunter oth Petra Fromme oth Raimund Fromme oth Syun-Ru Yeh oth Denis L Rousseau oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 30, Seite 8011 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:30 pages:8011 https://search.proquest.com/docview/1946419448 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 30 8011 |
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PQ20171228 (DE-627)OLC1998531325 (DE-599)GBVOLC1998531325 (PRQ)p933-2bee6702a4a769bee1c2ce50897d37deb242eb4f4bb979e5c1bb06f721e3e6bf0 (KEY)0583363920170000114003008011crystalstructureofcoboundcytochromecoxidasedetermi DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Izumi Ishigami verfasserin aut Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. Artifacts Heme Unwinding Bioenergetics Mitochondria Cytochrome-c oxidase Electron transfer Carbon monoxide Radiation damage Radiation Allosteric properties Cobalt Crystal structure Crystallography Femtosecond pH effects Translocation Protons Temperature Free energy X-ray crystallography Structural damage Light sources Cytochrome Synchrotron radiation Atmospheric chemistry Oxidase Iron Nadia A Zatsepin oth Masahide Hikita oth Chelsie E Conrad oth Garrett Nelson oth Jesse D Coe oth Shibom Basu oth Thomas D Grant oth Matthew H Seaberg oth Raymond G Sierra oth Mark S Hunter oth Petra Fromme oth Raimund Fromme oth Syun-Ru Yeh oth Denis L Rousseau oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 30, Seite 8011 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:30 pages:8011 https://search.proquest.com/docview/1946419448 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 30 8011 |
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PQ20171228 (DE-627)OLC1998531325 (DE-599)GBVOLC1998531325 (PRQ)p933-2bee6702a4a769bee1c2ce50897d37deb242eb4f4bb979e5c1bb06f721e3e6bf0 (KEY)0583363920170000114003008011crystalstructureofcoboundcytochromecoxidasedetermi DE-627 ger DE-627 rakwb eng 500 DE-101 570 AVZ LING fid BIODIV fid Izumi Ishigami verfasserin aut Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. Artifacts Heme Unwinding Bioenergetics Mitochondria Cytochrome-c oxidase Electron transfer Carbon monoxide Radiation damage Radiation Allosteric properties Cobalt Crystal structure Crystallography Femtosecond pH effects Translocation Protons Temperature Free energy X-ray crystallography Structural damage Light sources Cytochrome Synchrotron radiation Atmospheric chemistry Oxidase Iron Nadia A Zatsepin oth Masahide Hikita oth Chelsie E Conrad oth Garrett Nelson oth Jesse D Coe oth Shibom Basu oth Thomas D Grant oth Matthew H Seaberg oth Raymond G Sierra oth Mark S Hunter oth Petra Fromme oth Raimund Fromme oth Syun-Ru Yeh oth Denis L Rousseau oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 114(2017), 30, Seite 8011 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:114 year:2017 number:30 pages:8011 https://search.proquest.com/docview/1946419448 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 114 2017 30 8011 |
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Artifacts Heme Unwinding Bioenergetics Mitochondria Cytochrome-c oxidase Electron transfer Carbon monoxide Radiation damage Radiation Allosteric properties Cobalt Crystal structure Crystallography Femtosecond pH effects Translocation Protons Temperature Free energy X-ray crystallography Structural damage Light sources Cytochrome Synchrotron radiation Atmospheric chemistry Oxidase Iron |
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Izumi Ishigami @@aut@@ Nadia A Zatsepin @@oth@@ Masahide Hikita @@oth@@ Chelsie E Conrad @@oth@@ Garrett Nelson @@oth@@ Jesse D Coe @@oth@@ Shibom Basu @@oth@@ Thomas D Grant @@oth@@ Matthew H Seaberg @@oth@@ Raymond G Sierra @@oth@@ Mark S Hunter @@oth@@ Petra Fromme @@oth@@ Raimund Fromme @@oth@@ Syun-Ru Yeh @@oth@@ Denis L Rousseau @@oth@@ |
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Izumi Ishigami |
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Izumi Ishigami ddc 500 ddc 570 fid LING fid BIODIV misc Artifacts misc Heme misc Unwinding misc Bioenergetics misc Mitochondria misc Cytochrome-c oxidase misc Electron transfer misc Carbon monoxide misc Radiation damage misc Radiation misc Allosteric properties misc Cobalt misc Crystal structure misc Crystallography misc Femtosecond misc pH effects misc Translocation misc Protons misc Temperature misc Free energy misc X-ray crystallography misc Structural damage misc Light sources misc Cytochrome misc Synchrotron radiation misc Atmospheric chemistry misc Oxidase misc Iron Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature |
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500 DE-101 570 AVZ LING fid BIODIV fid Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature Artifacts Heme Unwinding Bioenergetics Mitochondria Cytochrome-c oxidase Electron transfer Carbon monoxide Radiation damage Radiation Allosteric properties Cobalt Crystal structure Crystallography Femtosecond pH effects Translocation Protons Temperature Free energy X-ray crystallography Structural damage Light sources Cytochrome Synchrotron radiation Atmospheric chemistry Oxidase Iron |
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Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature |
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Izumi Ishigami |
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crystal structure of co-bound cytochrome c oxidase determined by serial femtosecond x-ray crystallography at room temperature |
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Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature |
| abstract |
Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. |
| abstractGer |
Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. |
| abstract_unstemmed |
Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry. |
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Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1998531325</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230715082414.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">171125s2017 xx ||||| 00| ||eng c</controlfield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20171228</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1998531325</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1998531325</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)p933-2bee6702a4a769bee1c2ce50897d37deb242eb4f4bb979e5c1bb06f721e3e6bf0</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0583363920170000114003008011crystalstructureofcoboundcytochromecoxidasedetermi</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">500</subfield><subfield code="q">DE-101</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">570</subfield><subfield code="q">AVZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">LING</subfield><subfield code="2">fid</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">BIODIV</subfield><subfield code="2">fid</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Izumi Ishigami</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2017</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">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Cytochrome c oxidase (CcO), the terminal enzyme in the electron transfer chain, translocates protons across the inner mitochondrial membrane by harnessing the free energy generated by the reduction of oxygen to water. Several redox-coupled proton translocation mechanisms have been proposed, but they lack confirmation, in part from the absence of reliable structural information due to radiation damage artifacts caused by the intense synchrotron radiation. Here we report the room temperature, neutral pH (6.8), damage-free structure of bovine CcO (bCcO) in the carbon monoxide (CO)-bound state at a resolution of 2.3 Å, obtained by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser. As a comparison, an equivalent structure was obtained at a resolution of 1.95 Å, from data collected at a synchrotron light source. In the SFX structure, the CO is coordinated to the heme a3 iron atom, with a bent Fe-C-O angle of ~142°. In contrast, in the synchrotron structure, the Fe-CO bond is cleaved; CO relocates to a new site near CuB, which, in turn, moves closer to the heme a3 iron by ~0.38 Å. Structural comparison reveals that ligand binding to the heme a3 iron in the SFX structure is associated with an allosteric structural transition, involving partial unwinding of the helix-X between heme a and a3, thereby establishing a communication linkage between the two heme groups, setting the stage for proton translocation during the ensuing redox chemistry.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Artifacts</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Heme</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Unwinding</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Bioenergetics</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Mitochondria</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cytochrome-c oxidase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Electron transfer</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Carbon monoxide</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Radiation damage</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Radiation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Allosteric properties</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cobalt</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Crystal structure</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Crystallography</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Femtosecond</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">pH effects</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Translocation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protons</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Temperature</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Free energy</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">X-ray crystallography</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Structural damage</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Light sources</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cytochrome</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Synchrotron radiation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Atmospheric chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Oxidase</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Iron</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Nadia A Zatsepin</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Masahide Hikita</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Chelsie E Conrad</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Garrett Nelson</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Jesse D Coe</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Shibom Basu</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Thomas D Grant</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Matthew H Seaberg</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Raymond G Sierra</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Mark S Hunter</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Petra Fromme</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Raimund Fromme</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Syun-Ru Yeh</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Denis L Rousseau</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Proceedings of the National Academy of Sciences of the United States of America</subfield><subfield code="d">Washington, DC : NAS, 1877</subfield><subfield code="g">114(2017), 30, Seite 8011</subfield><subfield code="w">(DE-627)129505269</subfield><subfield code="w">(DE-600)209104-5</subfield><subfield code="w">(DE-576)014909189</subfield><subfield code="x">0027-8424</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:114</subfield><subfield code="g">year:2017</subfield><subfield code="g">number:30</subfield><subfield code="g">pages:8011</subfield></datafield><datafield tag="856" ind1="4" ind2="2"><subfield code="u">https://search.proquest.com/docview/1946419448</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_OLC</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-LING</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">FID-BIODIV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHY</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-CHE</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-DE-84</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-FOR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_59</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">114</subfield><subfield code="j">2017</subfield><subfield code="e">30</subfield><subfield code="h">8011</subfield></datafield></record></collection>
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