Transformation of the CuA redox site in cytochrome c oxidase into a mononuclear copper center.

Abstract:

:Subunit II of the aa3 type cytochrome c oxidase contains a binuclear copper center (CuA) which functions as the entry point for electrons donated by cytochrome c. We have introduced site-specific mutations in residues liganding the CuA center in the oxidase of the bacterium Paracoccus denitrificans; the purified, fully assembled enzyme complexes were analyzed by various techniques, including EPR, optical spectroscopy, and total-reflection X-ray fluorescence spectrometry, to determine metal to protein ratios. In the C216S mutant, the binuclear CuA site is transformed into a mononuclear copper center. In contrast to wild type, the C216S mutant does no longer exhibit the characteristic absorption band in the near-infrared region of the optical spectrum that has been assigned to CuA. These major changes in the CuA site of this mutant correlate with an almost complete loss in catalytic activity.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Zickermann V,Wittershagen A,Kolbesen BO,Ludwig B

doi

10.1021/bi962040e

subject

Has Abstract

pub_date

1997-03-18 00:00:00

pages

3232-6

issue

11

eissn

0006-2960

issn

1520-4995

pii

bi962040e

journal_volume

36

pub_type

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