scholarly journals Defining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with Leucine

Biochemistry ◽  
2009 ◽  
Vol 48 (39) ◽  
pp. 9174-9184 ◽  
Author(s):  
Moonsung Choi ◽  
Narayanasami Sukumar ◽  
Aimin Liu ◽  
Victor L. Davidson
Keyword(s):  
Axial Ligand ◽  
Copper Site ◽  
Type 1 Copper

An Axial Met Ligand at a Type 1 Copper Site is Preferable for Fast Electron Transfer

ChemBioChem ◽  
2004 ◽  
Vol 5 (11) ◽  
pp. 1579-1581 ◽  
Author(s):  
Mark D. Harrison ◽  
Christopher Dennison
Keyword(s):  
Electron Transfer ◽  
Fast Electron ◽  
Copper Site ◽  
Type 1 Copper

Effect of the Methionine Ligand on the Reorganization Energy of the Type-1 Copper Site of Nitrite Reductase

2007 ◽  
Vol 129 (3) ◽  
pp. 519-525 ◽  
Author(s):  
Hein J. Wijma ◽  
Iain MacPherson ◽  
Ole Farver ◽  
Elitza I. Tocheva ◽  
Israel Pecht ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Reorganization Energy ◽  
Copper Site ◽  
Type 1 Copper

Spectroscopic and Magnetic Studies of Human Ceruloplasmin:  Identification of a Redox-Inactive Reduced Type 1 Copper Site†

Biochemistry ◽  
1998 ◽  
Vol 37 (26) ◽  
pp. 9570-9578 ◽  
Author(s):  
Timothy E. Machonkin ◽  
Hua H. Zhang ◽  
Britt Hedman ◽  
Keith O. Hodgson ◽  
Edward I. Solomon
Keyword(s):  
Magnetic Studies ◽  
Copper Site ◽  
Type 1 Copper ◽  
Human Ceruloplasmin

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.

Effect of Cavity Size of Mesoporous Silica on Type 1 Copper Site Geometry in Pseudoazurin

2020 ◽  
Vol 93 (5) ◽  
pp. 630-636
Author(s):  
Akira Yamaguchi ◽  
Yurie Edanami ◽  
Takahide Yamaguchi ◽  
Yuuta Shibuya ◽  
Norihisa Fukaya ◽  
...  
Keyword(s):  
Mesoporous Silica ◽  
Cavity Size ◽  
Copper Site ◽  
Type 1 Copper

scholarly journals EXAFS of the type-1 copper site of rusticyanin

FEBS Letters ◽  
1990 ◽  
Vol 269 (1) ◽  
pp. 117-121 ◽  
Author(s):  
Steven D. Holt ◽  
Brian Piggott ◽  
W.John Ingledew ◽  
Martinus C. Feiters ◽  
Gregory P. Diakun
Keyword(s):  
Copper Site ◽  
Type 1 Copper

scholarly journals Pulse-radiolysis studies on the interaction of one-electron reduced species with blue oxidases. Reduction of type-2-copper-depleted ascorbate oxidase

1984 ◽  
Vol 222 (1) ◽  
pp. 65-70 ◽  
Author(s):  
P O'Neill ◽  
E M Fielden ◽  
L Avigliano ◽  
G Marcozzi ◽  
A Ballini ◽  
...  
Keyword(s):  
Pulse Radiolysis ◽  
Ascorbate Oxidase ◽  
Native Protein ◽  
Rate Determining Step ◽  
Type 1 Copper ◽  
Intramolecular Transfer ◽  
Reducing Equivalents

The interaction of one-electron reduced metronidazole (ArNO2.-) with native and Type-2-copper-depleted ascorbate oxidase were studied in buffered aqueous solution at pH 6.0 and 7.4 by using the technique of pulse radiolysis. With ArNO2.-, reduction of Type 1 copper of the native enzyme and of the Type-2-copper-depleted ascorbate oxidase occurs via a bimolecular step and at the same rate. Whereas the native protein accepts, in the absence of O2, 6-7 reducing equivalents, Type-2-copper-depleted ascorbate oxidase accepts only 3 reducing equivalents with stoichiometric reduction of Type 1 copper. On reaction of O2.- with ascorbate oxidase under conditions of [O2.-] much greater than [ascorbate oxidase], removal of Type 2 copper results in reduction of all the Type 1 copper atoms, in contrast with reduction of the equivalent of only one Type 1 copper atom in the holoprotein. From observations at 610 nm, the rate of reduction of ascorbate oxidase by O2.- is not dependent on the presence of Type 2 copper. For the holoprotein, no significant optical-absorption changes were observed at 330 nm. It is proposed that electrons enter the protein via Type 1 copper in a rate-determining step followed by a fast intramolecular transfer of electrons within the protein. For the Type-2-copper-depleted protein, intramolecular transfer within the protein, however, is slow or does not occur. In the presence of O2, it is also suggested that re-oxidation of the partially reduced holoprotein occurs at steady state, as inferred from the observations at 330 nm and 610 nm. The role of Type 2 copper in ascorbate oxidase is discussed in terms of its involvement in redistribution of electrons within the protein or structural considerations.

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