Energy-transfer studies of the distance between the high-affinity metal binding site and the colchicine and 8-anilino-1-naphthalenesulfonic acid binding sites on calf brain tubulin

Biochemistry ◽  
1988 ◽  
Vol 27 (5) ◽  
pp. 1508-1514 ◽  
Author(s):  
Larry D. Ward ◽  
Serge N. Timasheff
Keyword(s):  
Energy Transfer ◽  
Binding Site ◽  
Metal Binding ◽  
Binding Sites ◽  
Metal Binding Site ◽  
High Affinity ◽  
Brain Tubulin

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

Metal Binding to Pseudomonas aeruginosa Azurin: a Kinetic Investigation

2000 ◽  
Vol 55 (5-6) ◽  
pp. 347-354 ◽  
Author(s):  
Fabio Naro ◽  
Maria G. Tordi ◽  
Giorgio M. Giacometti ◽  
Francesco Tomei ◽  
Anna M. Timperio ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Metal Binding ◽  
Binding Sites ◽  
Fluorescence Emission ◽  
Uv Spectrum ◽  
Metal Binding Site ◽  
Metal Binding Sites ◽  
High Affinity ◽  
Redox Center ◽  
Sh Group

The interaction between azurin from Pseudomonas aeruginosa and Ag(I), Cu(II), Hg(II), was investigated as a function of protein state, i.e. apo-, reduced and oxidised azurin. Two different metal binding sites, characterized by two different spectroscopic absorbancies, were detected: one is accessible to Ag(I) and Cu(II) but not to Hg(II); the other one binds Ag(I) and Hg(II) but not copper. When added in stoichiometric amount, Ag(I) shows high affinity for the redox center of apo-azurin, to which it probably binds by the -SH group of Cys112; it can displace Cu(I) from reducedazurin, while it does not bind to the redox center of oxidizedazurin. Kinetic experiments show that Ag(I) binding to the reducedform is four times faster than binding to the apo-form. This result suggests that metal binding requires a conformational rearrangement of the active site of the azurin. Interaction of A g(I) or Hg(II) ions to the second metal binding site, induces typical changes of UV spectrum and quenching of fluorescence emission.

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

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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