Abstract:
:Cu,Zn superoxide dismutase from Photobacterium leiognathi has been cloned and expressed in Escherichia coli. The circular dichroism spectrum in the UV region of the recombinant protein indicates an higher content of random coil structure with respect to the eukaryotic enzymes. Investigation of the active site by optical, CD, and EPR spectroscopy indicates a different coordination geometry around the catalytic copper site with respect to the eukaryotic enzymes. In particular a different orientation of the metal bridging histidine is suggested. The pH dependence of the copper EPR spectrum shows the presence of a single equilibrium which is at least one unit lower than the pK value observed for the bovine enzyme. Despite such structural differences the catalytic rate of this enzyme is identical to that observed for the eukaryotic Cu,Zn superoxide dismutase, suggesting that the overall electric field distribution is similar to that observed in the eukaryotic enzymes.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Foti D,Lo Curto B,Cuzzocrea G,Stroppolo ME,Polizio F,Venanzi M,Desideri Adoi
10.1021/bi963020fsubject
Has Abstractpub_date
1997-06-10 00:00:00pages
7109-13issue
23eissn
0006-2960issn
1520-4995pii
bi963020fjournal_volume
36pub_type
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