Issue 4, 2011

Spring-loading the active site of cytochrome P450cam


A hydrogen bond network has been identified that adjusts protein-substrate contacts in cytochrome P450cam (CYP101A1). Replacing the native substrate camphor with adamantanone or norcamphor causes perturbations in NMR-detected NH correlations assigned to the network, which includes portions of a β sheet and an adjacent helix that is remote from the active site. A mutation in this helix reduces enzyme efficiency and perturbs the extent of substrate-induced spin state changes at the haem iron that accompany substrate binding. In turn, the magnitude of the spin state changes induced by alternate substrate binding parallel the NMR-detected perturbations observed near the haem in the enzyme active site.

Graphical abstract: Spring-loading the active site of cytochrome P450cam

  • This article is part of the themed collection: Cytochromes

Supplementary files

Article information

Article type
25 Oct 2010
09 Dec 2010
First published
24 Dec 2010

Metallomics, 2011,3, 339-343