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Crystal structures of oxidized and reduced stellacyanin from horseradish roots

Lookup NU author(s): Dr Dr MD Harrison Harrison, Professor Christopher Dennison

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Abstract

Umecyanin (UMC) is a type 1 copper-containing protein which originates from horseradish roots and belongs to the stellacyanin subclass of the phytocyanins, a ubiquitous family of plant cupredoxins. The crystal structures of Cu(II) and Cu(I) UMC have been determined at 1.9 and 1.8 Å, respectively. The protein has an overall fold similar to those of other phytocyanins. At the active site the cupric ion is coordinated by the Nδ1 atoms of His44 and His90, the Sγ of Cys85, and the Oε1 of Gln95 in a distorted tetrahedral geometry. Both His ligands are solvent exposed and are surrounded by nonpolar and polar side chains on the protein surface. Thus, UMC does not possess a distinct hydrophobic patch close to the active site in contrast to almost all other cupredoxins. UMC has a large surface acidic patch situated ∼10-30 Å from the active site. The structure of Cu(I) UMC is the first determined for a reduced phytocyanin and demonstrates that the coordination environment of the cuprous ion is more trigonal pyramidal. This subtle change in geometry is primarily due to the Cu-Nδ1(His44) and Cu-Oε1(Gln95) bond lengths increasing from 2.0 and 2.3 Å in Cu(II) UMC to 2.2 and 2.5 Å, respectively, in the reduced form, as a consequence of slight rotations of the His44 and Gln95 side chains. The limited structural changes upon redox interconversion at the active site of this stellacyanin are analogous to those observed in a typical type 1 copper site with an axial Met ligand and along with its surface features suggest a role for UMC in interprotein electron transfer.


Publication metadata

Author(s): Koch M, Velarde M, Harrison MD, Echt S, Fischer M, Messerschmidt A, Dennison C

Publication type: Article

Publication status: Published

Journal: Journal of the American Chemical Society

Year: 2005

Volume: 127

Issue: 1

Pages: 158-166

ISSN (print): 0002-7863

ISSN (electronic): 1943-2984

Publisher: American Chemical Society

URL: http://dx.doi.org/10.1021/ja046184p

DOI: 10.1021/ja046184p

PubMed id: 15631465


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