| Literature DB >> 6247336 |
S Kawato, E Sigel, E Carafoli, R J Cherry.
Abstract
A transient dichroism is detected after photolysis by a linearly polarized laser flash of the cytochrome oxidaseCO complex in bovine heart mitochondria, rat heart mitochondria, and bovine heart submitochondrial particles. A decay in the absorption anisotropy is characterized by a time constant of about 300 to 400 mus in both mitochondria and submitochondrial particles. Since vesicle tumbling in the time range less than 5 ms can be excluded in these experiments, we conclude that cytochrome oxidase rotates in the mitochondrial membrane with a relaxation time of several hundred microseconds. However, it is likely that only about one-half of cytochrome oxidase contributes to the observed decay, the remainder being relatively immobile.Entities:
Mesh:
Substances:
Year: 1980 PMID: 6247336
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157