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Vectorial nature of redox Bohr effects in bovine heart cytochrome c oxidase
Author(s) -
N. Capitanio,
Giuseppe Capitanio,
Emanuele De Nitto,
Sergio Papa
Publication year - 1997
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(97)01043-0
Subject(s) - cytochrome c oxidase , bohr effect , redox , chemistry , cytochrome c , electron transport complex iv , oxidation reduction , heme a , oxidase test , biochemistry , enzyme , mitochondrion , inorganic chemistry , hemoglobin , oxygen–haemoglobin dissociation curve
The vectorial nature of redox Bohr effects (redoxlinked pK shifts) in cytochrome c oxidase from bovine heart incorporated in liposomes has been analyzed. The Bohr effects linked to oxido‐reduction of heme a and Cu B display membrane vectorial asymmetry. This provides evidence for involvement of redox Bohr effects in the proton pump of the oxidase.