Spectroscopic characterization of recombinant Cu,Zn superoxide dismutase from Photobacterium leiognathi expressed in Escherichia coli: evidence for a novel catalytic copper binding site.

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

Biochemistry

journal_title

Biochemistry

authors

Foti D,Lo Curto B,Cuzzocrea G,Stroppolo ME,Polizio F,Venanzi M,Desideri A

doi

10.1021/bi963020f

subject

Has Abstract

pub_date

1997-06-10 00:00:00

pages

7109-13

issue

23

eissn

0006-2960

issn

1520-4995

pii

bi963020f

journal_volume

36

pub_type

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