Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase. |
| |
Authors: | G Buse T Soulimane M Dewor H E Meyer and M Blüggel |
| |
Institution: | Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany. |
| |
Abstract: | Following hints from X-ray data (Ostermeier C et al., 1997, Proc Natl Acad Sci USA 94:10547-10553; Yoshikawa S et al., 1998, Science 280: 1723-1729), chemical evidence is presented from four distantly related cytochrome-c oxidases for the existence of a copperB-coordinated His240-Tyr244) cross-link at the O2-activating Heme Fea3-CuB center in the catalytic subunit 1 of the enzyme. The early evolutionary invention of this unusual structure may have prevented damaging *OH-radical release at e(-)-transfer to dioxygen and thus have enabled O2 respiration. |
| |
Keywords: | cell respiration cytochrome-c oxidase histidine-tyrosine cross-link O2 activation oxygen radicals |
|
|