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Evidence for a copper-coordinated histidine–tyrosine cross-link in the active site of cytochrome oxidase

Published online by Cambridge University Press:  01 May 1999

GERHARD BUSE ,
TEWFIK SOULIMANE ,
MANFRED DEWOR ,
HELMUT E. MEYER  and
MARTIN BLÜGGEL
GERHARD BUSE
Affiliation:
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Pauwelsstrasse 30, 52074 Aachen, Germany
TEWFIK SOULIMANE
Affiliation:
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Pauwelsstrasse 30, 52074 Aachen, Germany
MANFRED DEWOR
Affiliation:
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Pauwelsstrasse 30, 52074 Aachen, Germany
HELMUT E. MEYER
Affiliation:
Institut für Immunologie, Ruhr, Universität Bochum, 44780 Bochum, Germany
MARTIN BLÜGGEL
Affiliation:
Institut für Immunologie, Ruhr, Universität Bochum, 44780 Bochum, Germany
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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 I of the enzyme. The early evolutionary invention of this unusual structure may have prevented demaging [bull ]OH-radical release at e−-transfer to dioxygen and thus have enabled O2 respiration.

Keywords

cell respirationcytochrome-c oxidasehistidine–tyrosine cross-linkO2 activationoxygen radicals
Type
Research Article
Information
Protein Science , Volume 8 , Issue 5 , May 1999 , pp. 985 - 990
Copyright
1999 The Protein Society

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