The carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site-Reference-Cited by-同舟云学术

The carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site

Published:2019-05 Issue:19 Volume:294 Page:7601-7614
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Alfano Marila^ORCID,Pérard Julien,Carpentier Philippe,Basset Christian,Zambelli Barbara,Timm Jennifer^ORCID,Crouzy Serge,Ciurli Stefano^ORCID,Cavazza Christine^ORCID

Funder

EC | Horizon 2020 Framework Programme

Agence Nationale de la Recherche

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

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4. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster;Dobbek;Science,2001

5. Nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: in vivo and in vitro activation by exogenous nickel (hydrogenase/iron-sulfur protein/electron paramagnetic resonance);Bonam;Biochemistry,1988

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