Functional importance of Glutamate-445 and Glutamate-99 in proton-coupled electron transfer during oxygen reduction by cytochrome bd from Escherichia coli.

Abstract excerpt

The recent X-ray structure of the cytochrome bd respiratory oxygen reductase showed that two of the three heme components, heme d and heme b595, have glutamic acid as an axial ligand. No other native heme proteins are known to have glutamic acid axial ligands. In this work, site-directed mutagenesis is used to probe the roles of these glutamic acids, E445 and E99 in the E. coli enzyme. It is concluded that...

Topics

• Cell Respiration
• Cytochrome b Group
• Cytochromes
• Electron Transport
• Electron Transport Chain Complex Proteins
• Electrons
• Escherichia coli
• Escherichia coli Proteins
• Glutamic Acid
• Heme