Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published February 12, 1992 | public
Journal Article

Ligand photodissociation and recombination dynamics of ferrous cytochrome c peroxidase at alkaline pH

Abstract

The dynamics associated with ligand photodissociation and ligand binding provide an avenue through which information concerning conformational interactions involving the active site of heme proteins may be obtained. To date, most time-resolved spectroscopic investigations have involved exogenous π-acceptor ligands such as CO, O_2, and NO. In fact, until very recently hexacoordinate low-spin hemes with strong-field σ-donor ligands were considered to be largely nonphotolabile. Magda and coworkers have, however, demonstrated that both cytochrome c and cytochrome b_5 exhibit photodissociation of nitrogenous ligands on a very fast (< 100 ps) time scale. Photodissociation of a σ ligand has also been implicated in the photodynamics of the cytochrome a_3 distal heme pocket in cytochrome c oxidase. This study characterizes the dynamics of the low-spin alkaline form of ferrous cytochrome c peroxidase (CCP) subsequent to heme photodissociation.

Additional Information

© 1992 American Chemical Society. Received October 18, 1991. We gratefully acknowledge the financial support of the National Institutes of Health [GM33330 (M.R.O.) and GM22432 (S.I.C.)].

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023