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Nickel-Induced Oligomerization of the Histidine-Rich Metallochaperone CooJ from Rhodospirillum Rubrum

Univ. Grenoble Alpes, CEA, CNRS, CBM, F-38000 Grenoble, France
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Inorganics 2019, 7(7), 84; https://doi.org/10.3390/inorganics7070084
Received: 27 May 2019 / Revised: 19 June 2019 / Accepted: 25 June 2019 / Published: 1 July 2019
(This article belongs to the Special Issue Bioinorganic Chemistry of Nickel)
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Abstract

[NiFe]-carbon monoxide dehydrogenase reversibly catalyzes the oxidation of CO to CO2. Its active site is a unique NiFe4S4 cluster, known as C-cluster. In Rhodospirillum rubrum, three nickel-dependent proteins, CooC, CooT and CooJ are required for Ni insertion into the active site. Among them, CooJ is a histidine-rich protein, containing two distinct and spatially separated Ni(II)-binding sites: a strictly conserved N-terminal site and a variable histidine tail at the C-terminus. Here, using biophysical techniques, we study the behavior of the protein upon Ni(II) addition. Using circular dichroism and chemical denaturation, we show that the binding of Ni(II) to the protein increases its stability. Moreover, high-order oligomers are formed through nickel–histidine tail interactions, both in vitro and in cellulo, via a dynamical and reversible process. View Full-Text
Keywords: histidine-rich protein; carbon monoxide dehydrogenase; nickel chaperone; nickel-induced oligomerization histidine-rich protein; carbon monoxide dehydrogenase; nickel chaperone; nickel-induced oligomerization
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Alfano, M.; Pérard, J.; Cavazza, C. Nickel-Induced Oligomerization of the Histidine-Rich Metallochaperone CooJ from Rhodospirillum Rubrum. Inorganics 2019, 7, 84.

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