Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum

Authors: Maher, Megan; Cross, Maddalena; Wilce, Matthew C. J.; Guss, J. Mitchell; Wedd, Anthony G.

Source: Acta Crystallographica Section D, Volume 60, Number 2, 1 February 2004 , pp. 298-303(6)

Publisher: Blackwell Publishing

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe atom present in the Fe(S-Cys)₄ site of the native form of the protein was exchanged in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin crystallized in space group R3 and were isomorphous with the native protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites with geometries similar to that of the Fe form (effective D_2d local symmetry), as did the Cd and Hg proteins, but with a significant expansion of the metal-sulfur bond lengths. A knowledge of these structures contributes to a molecular understanding of the function of this simple iron-sulfur electron-transport protein.

Keywords: rubredoxins; iron-sulfur; Clostridium pasteurianum

Document Type: Research article

DOI: 10.1107/S090744490302794X

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.16 plus tax Refund Policy