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Cover Picture: Hot‐Spot Residues in the Cytochrome P450cam–Putidaredoxin Binding Interface (ChemBioChem 1/2014)
Author(s) -
Hiruma Yoshitaka,
Gupta Ankur,
Kloosterman Alexander,
Olijve Caroline,
Ölmez Betül,
Hass Mathias A. S.,
Ubbink Marcellus
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390069
Subject(s) - chemistry , ferredoxin , cytochrome , cover (algebra) , heme , monooxygenase , mutagenesis , electron transfer , hemeprotein , stereochemistry , crystallography , cytochrome p450 , photochemistry , biochemistry , enzyme , mutation , mechanical engineering , engineering , gene
The cover picture shows several hot‐spot residues at the binding interface of the heme‐containing monooxygenase cytochrome P450cam and putidaredoxin, a ferredoxin that contains a [2 Fe–2 S] cluster. The cartoon on the right represents the overall structure of P450cam. For more details of how site‐directed mutagenesis, kinetic measurements, and NMR studies have shown the effects (or not) of the interactions of polar residues on partner recognition and electron transfer rates, see the paper by M. Ubbink et al. on p. 80 ff. The image was produced by Mitsuko Nakao.