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A cytochrome c oxidase proton pumping mechanism that excludes the O 2 reduction site
Author(s) -
Yoshikawa Shinya
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01098-6
Subject(s) - cytochrome c oxidase , chemistry , reduction (mathematics) , mechanism (biology) , proton , photochemistry , stereochemistry , biochemistry , physics , enzyme , nuclear physics , quantum mechanics , geometry , mathematics
A redox‐coupled conformational change in Asp51 of subunit I and a hydrogen‐bond network connecting Asp51 with the matrix surface have been deduced from X‐ray structures of bovine heart cytochrome c oxidase. This has provided evidence that Asp51 may play a role in the proton pumping process. However, the lack of complete conservation of a residue analogous to Asp51, the inclusion of a peptide bond in the hydrogen‐bonding network and the lack of apparent involvement of the O 2 reduction site have been used as arguments against the involvement of Asp51 in the mechanism of proton pumping. This minireview re‐examines these arguments.