Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter.

Article Details

Citation

Park IS, Hausinger RP

Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter.

Science. 1995 Feb 24;267(5201):1156-8.

PubMed ID
7855593 [ View in PubMed
]
Abstract

Assembly of protein metallocenters is not well understood. Urease offers a tractable system for examination of this process. Formation of the urease metallocenter in vivo is known to require four accessory proteins: UreD, postulated to be a urease-specific molecular chaperone; UreE, a nickel(II)-binding protein; and UreF and UreG, of unknown function. Activation of purified Klebsiella aerogenes urease apoprotein was accomplished in vitro by providing carbon dioxide (half-maximal activation at approximately 0.2 percent carbon dioxide) in addition to nickel ion. Activation coincided with carbon dioxide incorporation into urease in a pH-dependent reaction (pKa > or = 9, where Ka is the acid constant). The concentration of carbon dioxide also affected the amount of activation of UreD-urease apoprotein complexes. These results suggest that carbon dioxide binding to urease apoprotein generates a ligand that facilitates productive nickel binding.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Urease subunit alphaP18314Details