The metal selectivity of a short peptide maquette imitating the high-affinity metal-binding site of E. coli HypB

2012 ◽  
Vol 41 (26) ◽  
pp. 7876 ◽  
Author(s):  
Colin D. Douglas ◽  
Alistair V. Dias ◽  
Deborah B. Zamble
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
Short Peptide ◽  
E Coli ◽  
High Affinity ◽  
Metal Selectivity

scholarly journals Zinc- and iron-dependent cytosolic metallo-β-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site

2004 ◽  
Vol 385 (1) ◽  
pp. 145-153 ◽  
Author(s):  
Oliver SCHILLING ◽  
Andreas VOGEL ◽  
Brenda KOSTELECKY ◽  
Hugo NATAL da LUZ ◽  
Daniel SPEMANN ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Dissociation Constants ◽  
Zinc Binding ◽  
Titration Calorimetry ◽  
Good Correspondence ◽  
Metal Binding Site ◽  
E Coli ◽  
Metal Ligands ◽  
Metal Selectivity

ZiPD (zinc phosphodiesterase; synonyms are ElaC, ecoZ, RNaseZ and 3′ tRNase) and the iron-dependent redox enzyme FlRd (flavorubredoxin) from Escherichia coli represent prototypical cases of proteins sharing the metallo-β-lactamase fold that require strict metal selectivity for catalytic activity, yet their metal selectivity has only been partially understood. In contrast with hydrolytic metallo-β-lactamase proteins, iron-dependent FlRd-like enzymes have an atypical glutamate ligand, which replaces one otherwise conserved histidine ligand. X-ray absorption spectroscopy revealed that the FlRd metallo-β-lactamase domain is capable of incorporating two zinc ions into the binuclear metal-binding site. Zinc dissociation constants, determined by isothermal titration calorimetry are similar for zinc binding to E. coli ZiPD (Kd1=2.2±0.2 μM and Kd2=23.0±0.6 μM) and to the E. coli FlRd metallo-β-lactamase domain (Kd1=0.7±0.1 μM and Kd2=26.0±0.1 μM). In good correspondence, apo-ZiPD requires incubation with 10 μM zinc for full reconstitution of the phosphodiesterase activity. Accordingly, metal selectivity of ZiPD and FlRd only partially relies on first shell metal ligands. Back mutation of the atypical glutamate in FlRd to a histidine unexpectedly resulted in an increased first zinc dissociation constant (Kd1=30±4 μM and Kd2=23±2 μM). In combination with a recent mutational study on ZiPD [Vogel, Schilling and Meyer-Klaucke (2004) Biochemistry 43, 10379–10386], we conclude that the atypical glutamate does not guide metal selectivity of the FlRd metallo-β-lactamase domain but suppresses possible hydrolytic cross-activity.

scholarly journals Metal Preference At The Second Metal Binding Site Of E. coli NikR

2009 ◽  
Vol 96 (3) ◽  
pp. 58a
Author(s):  
Christine M. Phillips ◽  
Paul S. Nerenberg ◽  
Catherine L. Drennan ◽  
Collin M. Stultz
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
E Coli

Characterization of Ligands of a High-Affinity Metal-Binding Site in the Latent Chloroplast F1-ATPase by EPR Spectroscopy of Bound VO2+

Biochemistry ◽  
1994 ◽  
Vol 33 (16) ◽  
pp. 4910-4917 ◽  
Author(s):  
Andrew L. P. Houseman ◽  
Lola Morgan ◽  
Russell LoBrutto ◽  
Wayne D. Frasch
Keyword(s):  
Binding Site ◽  
Epr Spectroscopy ◽  
Metal Binding ◽  
Metal Binding Site ◽  
F1 Atpase ◽  
High Affinity

High-Affinity Metal-Binding Site in Beef Heart Mitochondrial F1ATPase:  An EPR Spectroscopy Study†

Biochemistry ◽  
2004 ◽  
Vol 43 (41) ◽  
pp. 13214-13224 ◽  
Author(s):  
Alfonso Zoleo ◽  
Stefania Contessi ◽  
Giovanna Lippe ◽  
Luca Pinato ◽  
Marina Brustolon ◽  
...  
Keyword(s):  
Binding Site ◽  
Epr Spectroscopy ◽  
Metal Binding ◽  
Beef Heart ◽  
Spectroscopy Study ◽  
Metal Binding Site ◽  
High Affinity

scholarly journals Identification and characterization of a novel high affinity metal-binding site in the hammerhead ribozyme

RNA ◽  
1999 ◽  
Vol 5 (8) ◽  
pp. 1099-1104 ◽  
Author(s):  
MARK R. HANSEN ◽  
JEAN-PIERRE SIMORRE ◽  
PAUL HANSON ◽  
VICTOR MOKLER ◽  
LAURENT BELLON ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Hammerhead Ribozyme ◽  
Metal Binding Site ◽  
High Affinity ◽  
Identification And Characterization

scholarly journals Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.

1992 ◽  
Vol 11 (9) ◽  
pp. 3209-3217 ◽  
Author(s):  
J. van der Oost ◽  
P. Lappalainen ◽  
A. Musacchio ◽  
A. Warne ◽  
L. Lemieux ◽  
...  
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
Quinol Oxidase ◽  
E Coli ◽  
Cytochrome O ◽  
A Subunit ◽  
Copper Sites

Unraveling the Substrate−Metal Binding Site of Ferrochelatase:  An X-ray Absorption Spectroscopic Study†

Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 4809-4818 ◽  
Author(s):  
Gloria C. Ferreira ◽  
Ricardo Franco ◽  
Arianna Mangravita ◽  
Graham N. George
Keyword(s):  
Spectroscopic Study ◽  
Binding Site ◽  
Metal Binding ◽  
Metal Binding Site ◽  
X Ray ◽  
Substrate Metal ◽  
X Ray Absorption
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