title: Spring-loading the active site of cytochrome P450cam.
abstract: A hydrogen bond network has been identified that adjusts protein-substrate contacts in cytochrome P450(cam) (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.
authors.affiliation: Department of Chemistry, MS 015, Brandeis University, 415 South St, Waltham, MA 02454-9110, USA.
authors.forename: Marina
authors.initials: M
authors.lastname: Dang
authors.forename: Susan Sondej
authors.initials: SS
authors.lastname: Pochapsky
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Pochapsky
mesh_terms: D000595:Amino Acid Sequence; D019475:Camphor 5-Monooxygenase / Q000737:chemistry*; D020134:Catalytic Domain; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000737:chemistry / Q000201:enzymology*; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D019475:Camphor 5-Monooxygenase