A Dynamic Zn Site in Helicobacter pylori HypA: A Potential Mechanism for Metal-Specific Protein Activity

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/ja066958x· OSTI ID:930312

Kennedy, D; Herbst, R; Iwig, J; Chivers, P; Maroney, M

HypA is an accessory protein and putative metallochaperone that is critical for supplying nickel to the active site of NiFe hydrogenases. In addition to binding Ni(II), HypA is known to contain a Zn site that has been suggested to play a structural role. X-ray absorption spectroscopy has been used to show that the Zn site changes structure upon binding nickel, from a S{sub 3}(O/N)-donor ligand environment to an S{sub 4}-donor ligand environment. This provides a potential mechanism for discriminating Ni(II) from other divalent metal ions. The Ni(II) site is shown to be a six-coordinate complex composed of O/N-donors including two histidines. As such, it resembles the nickel site in UreE, a nickel metallochaperone involved in nickel incorporation into urease.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 930312
• Report Number(s): BNL--81022-2008-JA
• Journal Information: Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Vol. 129; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
DYNAMICS
ENVIRONMENT
HYDROGENASES
IONS
LIGANDS
METALS
NICKEL
PROTEINS
UREASE
national synchrotron light source