Phosphate ester hydrolysis is catalyzed by a bacterial transferrin: potential implications for in vivo iron transport mechanisms.

Journal Article (Journal Article)

Two synergistic anions, p-nitrophenyl phosphate ester (NPP) and SO(4)(2-), were found to form new stable assemblies with Fe(3+) and a bacterial transferrin, FbpA (FbpA=ferric binding protein). Fe(3+)FbpA-SO(4) undergoes rapid anion exchange in the presence of NPP to form Fe(3+)FbpA-NPP. Formation of Fe(3+)FbpA-NPP was found to accelerate the rate of hydrolysis of the bound phosphate ester (k(hyd)=1.6 x 10(-6) s(-1) at 25 degrees C and pH 6.5) by >10(3) fold over the uncatalyzed reaction. These findings suggest a dual function for FbpA in vivo: transport of Fe(3+) across the periplasmic space to the inner membrane in certain gram-negative bacteria and hydrolysis of periplasmic polyphosphates.

Full Text

Duke Authors

Cited Authors

  • Dhungana, S; Anderson, DS; Mietzner, TA; Crumbliss, AL

Published Date

  • November 2004

Published In

Volume / Issue

  • 98 / 11

Start / End Page

  • 1975 - 1977

PubMed ID

  • 15522424

Electronic International Standard Serial Number (EISSN)

  • 1873-3344

International Standard Serial Number (ISSN)

  • 0162-0134

Digital Object Identifier (DOI)

  • 10.1016/j.jinorgbio.2004.08.004


  • eng