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Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase.

ABSTRACT: Cytochrome c oxidase (CcO) is part of the respiratory chain and contributes to the electrochemical membrane gradient in mitochondria as well as in many bacteria, as it uses the energy released in the reduction of oxygen to pump protons across an energy-transducing biological membrane. Here, we use time-resolved serial femtosecond crystallography to study the structural response of the active site upon flash photolysis of carbon monoxide (CO) from the reduced heme a3 of ba3-type CcO. In contrast with the aa3-type enzyme, our data show how CO is stabilized on CuB through interactions with a transiently ordered water molecule. These results offer a structural explanation for the extended lifetime of the CuB-CO complex in ba3-type CcO and, by extension, the extremely high oxygen affinity of the enzyme.

SUBMITTER: Safari C 

PROVIDER: S-EPMC10708180 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

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Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome <i>c</i> oxidase.

Safari Cecilia C   Ghosh Swagatha S   Andersson Rebecka R   Johannesson Jonatan J   Båth Petra P   Uwangue Owens O   Dahl Peter P   Zoric Doris D   Sandelin Emil E   Vallejos Adams A   Nango Eriko E   Tanaka Rie R   Bosman Robert R   Börjesson Per P   Dunevall Elin E   Hammarin Greger G   Ortolani Giorgia G   Panman Matthijs M   Tanaka Tomoyuki T   Yamashita Ayumi A   Arima Toshi T   Sugahara Michihiro M   Suzuki Mamoru M   Masuda Tetsuya T   Takeda Hanae H   Yamagiwa Raika R   Oda Kazumasa K   Fukuda Masahiro M   Tosha Takehiko T   Naitow Hisashi H   Owada Shigeki S   Tono Kensuke K   Nureki Osamu O   Iwata So S   Neutze Richard R   Brändén Gisela G  

Science advances 20231208 49

Cytochrome <i>c</i> oxidase (C<i>c</i>O) is part of the respiratory chain and contributes to the electrochemical membrane gradient in mitochondria as well as in many bacteria, as it uses the energy released in the reduction of oxygen to pump protons across an energy-transducing biological membrane. Here, we use time-resolved serial femtosecond crystallography to study the structural response of the active site upon flash photolysis of carbon monoxide (CO) from the reduced heme <i>a<sub>3</sub></  ...[more]

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