The site of the redox-linked proton pump in eukaryotic cytochrome c oxidases.

Published

Journal Article

The electronic spectra of fully oxidized derivatives of some cytochrome c oxidase preparations are distinctly pH dependent. In general, the observed spectral shifts are greater in the case of pulsed derivatives compared to resting preparations and also, greater for preparations of the enzyme from shark skeletal muscle compared to beef heart. The low temperature near-infrared magnetic circular dichroism spectrum of the fully oxidized shark enzyme is not pH dependent in the experimental range, indicating the sensitivity of the visible region electronic spectrum to variation in pH to be due principally to changes at the heme a3-CuB chromophore. The results are discussed in relation to proposed mechanisms of proton translocation in cytochrome c oxidase.

Full Text

Duke Authors

Cited Authors

  • Holm, DE; Godette, G; Bonaventura, J; Bonaventura, C; Peterson, J

Published Date

  • August 1995

Published In

Volume / Issue

  • 370 / 1-2

Start / End Page

  • 53 - 58

PubMed ID

  • 7649304

Pubmed Central ID

  • 7649304

Electronic International Standard Serial Number (EISSN)

  • 1873-3468

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(95)00791-7

Language

  • eng