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Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum.

Maher M, Cross M, Wilce MC, Guss JM, Wedd AG
Acta Crystallogr D Biol Crystallogr 60 298-303 (2004)
Related entries: 1r0f, 1r0g, 1r0h, 1r0i

Cited: 15 times
EuropePMC logo PMID: 14747706

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.

Articles - 1r0j mentioned but not cited (2)

  1. Experimental and DFT Investigations Reveal the Influence of the Outer Coordination Sphere on the Vibrational Spectra of Nickel-Substituted Rubredoxin, a Model Hydrogenase Enzyme. Slater JW, Marguet SC, Cirino SL, Maugeri PT, Shafaat HS. Inorg Chem 56 3926-3938 (2017)
  2. An NMR structural study of nickel-substituted rubredoxin. Goodfellow BJ, Duarte IC, Macedo AL, Volkman BF, Nunes SG, Moura I, Markley JL, Moura JJ. J Biol Inorg Chem 15 409-420 (2010)


Reviews citing this publication (1)

  1. Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. Meyer J. J Biol Inorg Chem 13 157-170 (2008)

Articles citing this publication (12)



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