Conformational Heterogeneity and the Affinity of Substrate Molecular Recognition by Cytochrome P450cam.

ABSTRACT: The broad and variable substrate specificity of cytochrome P450 enzymes makes them a model system for studying the determinants of protein molecular recognition. The archetypal cytochrome P450cam (P450cam) is a relatively specific P450, a feature once attributed to the high rigidity of its active site. However, increasingly studies have provided evidence of the importance of conformational changes to P450cam activity. Here we used infrared (IR) spectroscopy to investigate the molecular recognition of P450cam. Toward this goal, and to assess the influence of a hydrogen bond (H-bond) between active site residue Y96 and substrates, two variants in which Y96 is replaced by a cyanophenyl (Y96CNF) or phenyl (Y96F) group were characterized in complexes with the substrates camphor, isoborneol, and

SUBMITTER: Basom EJ 

PROVIDER: S-EPMC5816979 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature