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

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

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

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.

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
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