Creation of a Type 1 Blue Copper Site within a de Novo Coiled-Coil Protein Scaffold

2010 ◽  
Vol 132 (51) ◽  
pp. 18191-18198 ◽  
Author(s):  
Daigo Shiga ◽  
Daisuke Nakane ◽  
Tomohiko Inomata ◽  
Yasuhiro Funahashi ◽  
Hideki Masuda ◽  
...  
Keyword(s):  
De Novo ◽  
Coiled Coil ◽  
Blue Copper ◽  
Protein Scaffold ◽  
Copper Site

scholarly journals An e.p.r. study of the non-equivalence of the copper sites of caeruloplasmin

1986 ◽  
Vol 238 (1) ◽  
pp. 291-295 ◽  
Author(s):  
L Calabrese ◽  
M Carbonaro
Keyword(s):  
Slow Phase ◽  
Copper Binding ◽  
Blue Copper ◽  
Sequence Of Events ◽  
Copper Site ◽  
Hyperfine Splitting Constant ◽  
Type 1 Copper ◽  
Splitting Constant

The two Type 1 (blue) copper-binding sites of caeruloplasmin were spectroscopically differentiated by the kinetic analysis of the e.p.r. spectra during the redox cycle. One blue copper, with a hyperfine splitting constant (A parallel) of 6.8 mT, which was rapidly reduced, was not reoxidized by oxygen, whereas it was reoxidized by H2O2. The other blue copper (A parallel = 5.8 mT), which was reduced slowly, was rapidly reoxidized by either oxygen or H2O2. A conformational change of the Type 2 copper was concomitant with the fast reduction of Type 1 copper, whereas its reduction occurred during the slow phase. This sequence of events was reversed in the reoxidation step, that is, the Type 2 copper reappeared rapidly as the species with altered conformation and reverted to the symmetry typical of the native state in the slow phase. The specific reaction of a blue-copper site with the H2O2 can tentatively be related to the established ability of caeruloplasmin to prevent ‘oxidative’ attack of proteins and lipids.

scholarly journals Modulating the copper–sulfur interaction in type 1 blue copper azurin by replacing Cys112 with nonproteinogenic homocysteine

2014 ◽  
Vol 1 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Kevin M. Clark ◽  
Yang Yu ◽  
Wilfred A. van der Donk ◽  
Ninian J. Blackburn ◽  
Yi Lu
Keyword(s):  
Amino Acid ◽  
Blue Copper ◽  
Copper Site ◽  
Type 1 Copper

Replacement of conserved Cys112 in azurin with a nonproteinogenic amino acid homocysteine affords a type-1 copper site with decreased Cu–SCys covalency.

Loop-Directed Mutagenesis of the Blue Copper Protein Amicyanin fromParacoccus versutusand Its Effect on the Structure and the Activity of the Type-1 Copper Site

2000 ◽  
Vol 122 (2) ◽  
pp. 204-211 ◽  
Author(s):  
Christian Buning ◽  
Gerard W. Canters ◽  
Peter Comba ◽  
Christopher Dennison ◽  
Lars Jeuken ◽  
...  
Keyword(s):  
Directed Mutagenesis ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Copper Site ◽  
Type 1 Copper

A pH-dependent resonance raman study on blue copper site of cucumber stellacyanin and its GLN→MET variant

1997 ◽  
Vol 67 (1-4) ◽  
pp. 49
Author(s):  
G. Fraczkiewicz ◽  
A.R. Nersissian ◽  
J.P. Hart ◽  
J.S. Valentine ◽  
R.S. Czernuszewicz
Keyword(s):  
Resonance Raman ◽  
Blue Copper ◽  
Copper Site ◽  
Raman Study ◽  
Ph Dependent

scholarly journals Low-temperature resonance-Raman spectra of Japanese-lacquer-tree (Rhus vernicifera) laccase, type-2-copper-depleted laccase and H2O2-treated type-2-copper-depleted laccase

1983 ◽  
Vol 213 (2) ◽  
pp. 503-506 ◽  
Author(s):  
G Musci ◽  
A Desideri ◽  
L Morpurgo ◽  
A Garnier-Suillerot ◽  
L Tosi
Keyword(s):  
Raman Spectra ◽  
Strong Dependence ◽  
Resonance Raman ◽  
Local Symmetry ◽  
Structural Rearrangements ◽  
Blue Copper ◽  
Copper Site ◽  
Resonance Raman Spectra ◽  
Rhus Vernicifera

Resonance-Raman spectra of Japanese-lacquer-tree (Rhus vernicifera) laccase, type-2-copper-depleted laccase and the latter form treated with H2O2 were measured in liquid and frozen solution, on excitation into the 600 nm absorption band. Significant changes in intensity and/or frequency of the bands lying in the 370-430 cm-1 region were observed on freezing, indicating local structural rearrangements taking place at the blue copper site. These findings corroborate previous suggestions based on e.p.r. measurements and redox data [Morpurgo, Calabrese, Desideri & Rotilio (1981) Biochem. J. 193, 639-642]. They show the strong dependence of the physical properties of blue copper centres on local symmetry. Some conclusions on the origin of the Raman bands are also drawn.

Coiled-Coil Motif as a Structural Basis for the Interaction of HTLV Type 1 Tax with Cellular Cofactors

2000 ◽  
Vol 16 (16) ◽  
pp. 1689-1694 ◽  
Author(s):  
Abel C. S. Chun ◽  
Yuan Zhou ◽  
Chi-Ming Wong ◽  
Hsiang-Fu Kung ◽  
Kuan-Teh Jeang ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Structural Basis

scholarly journals Spectroscopic and Density Functional Theory Studies of the Blue−Copper Site in M121SeM and C112SeC Azurin:  Cu−Se Versus Cu−S Bonding

2008 ◽  
Vol 130 (12) ◽  
pp. 3866-3877 ◽  
Author(s):  
Ritimukta Sarangi ◽  
Serge I. Gorelsky ◽  
Lipika Basumallick ◽  
Hee Jung Hwang ◽  
Russell C. Pratt ◽  
...  
Keyword(s):  
Density Functional Theory ◽  
Density Functional ◽  
Functional Theory ◽  
Blue Copper ◽  
Copper Site

Tuning the geometries of a de novo blue copper protein by axial interactions

2012 ◽  
Vol 17 (7) ◽  
pp. 1025-1031 ◽  
Author(s):  
Daigo Shiga ◽  
Yusuke Hamano ◽  
Misato Kamei ◽  
Yasuhiro Funahashi ◽  
Hideki Masuda ◽  
...  
Keyword(s):  
De Novo ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein

Removing an Interhelical Salt Bridge Abolishes Coiled-Coil Formation in a de Novo Designed Peptide

2002 ◽  
Vol 137 (1-2) ◽  
pp. 65-72 ◽  
Author(s):  
Markus Meier ◽  
Ariel Lustig ◽  
Ueli Aebi ◽  
Peter Burkhard
Keyword(s):  
De Novo ◽  
Coiled Coil ◽  
Salt Bridge
Sign in / Sign up

Export Citation Format

Share Document