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Science 24 February 1995:
Vol. 267. no. 5201, pp. 1156 - 1158
DOI: 10.1126/science.7855593
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Articles
Science, Vol 267, Issue 5201, 1156-1158
Copyright © 1995 by American Association for the Advancement of Science
Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter
IS Park
and
RP Hausinger
Department of Microbiology, Michigan State University, East Lansing 48824.
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.
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- At last--the crystal structure of urease.
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