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
Biochemistryjournal_title
Biochemistryauthors
Zickermann V,Wittershagen A,Kolbesen BO,Ludwig Bdoi
10.1021/bi962040esubject
Has Abstractpub_date
1997-03-18 00:00:00pages
3232-6issue
11eissn
0006-2960issn
1520-4995pii
bi962040ejournal_volume
36pub_type
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