Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase.
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.
Buse
G
G
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany. GerhardBuse@post.rwth-aachen.de
Soulimane
T
T
Dewor
M
M
Meyer
H E
HE
Blüggel
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003300:Copper / Q000737:chemistry*; D003576:Electron Transport Complex IV / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D013058:Mass Spectrometry; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010101:Oxygen Consumption; D010231:Paracoccus denitrificans / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry*
D014443:Tyrosine; D006639:Histidine; D003300:Copper; D003576:Electron Transport Complex IV