Ontology highlight
ABSTRACT:
SUBMITTER: Zhong F
PROVIDER: S-EPMC3903235 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Zhong Fangfang F Lisi George P GP Collins Daniel P DP Dawson John H JH Pletneva Ekaterina V EV
Proceedings of the National Academy of Sciences of the United States of America 20140107 3
Cysteine-bound hemes are key components of many enzymes and biological sensors. Protonation (deprotonation) of the Cys ligand often accompanies redox transformations of these centers. To characterize these phenomena, we have engineered a series of Thr78Cys/Lys79Gly/Met80X mutants of yeast cytochrome c (cyt c) in which Cys78 becomes one of the axial ligands to the heme. At neutral pH, the protonation state of the coordinated Cys differs for the ferric and ferrous heme species, with Cys binding as ...[more]