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X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms

Atsuhiro Shimada, Yuki Etoh, Rika Kitoh-Fujisawa, Ai Sasaki, Kyoko Shinzawa‐Itoh, Takeshi Hiromoto, Eiki Yamashita, Kazumasa Muramoto, Tomitake Tsukihara, Shinya Yoshikawa

2020Journal of Biological Chemistry27 citationsDOIOpen Access PDF

Abstract

state, preventing its detection, consistent with the unexpected Raman results. The H-pathway structures of both intermediates indicated that during proton-pumping from the hydrogen-bond network to the P-side, a transmembrane helix closes the water channel connecting the N-side with the hydrogen-bond network, facilitating unidirectional proton-pumping during the P-to-F transition.

Topics & Concepts

ChemistryCatalytic cycleProtonRaman spectroscopyCatalysisCytochrome c oxidasePhotochemistryMoleculeHydrogen bondCrystallographyStereochemistryEnzymePhysicsBiochemistryOpticsQuantum mechanicsOrganic chemistryPhotosynthetic Processes and MechanismsPhotoreceptor and optogenetics researchSpectroscopy and Quantum Chemical Studies
X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms | Litcius