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Other blue copper protein redox potentials start around +310 mV and reach up to +680 mV. [2] A mutant cucumber stellacyanin was created by replacing the glutamine axial ligand (a ligand which all other blue proteins contain) with a methionine (Q99M) and purified. This was achieved through Polymerase Chain Reaction (PCR). The mutated ...
An example is the Cu 2+/+ aquo complex, which is 5 x 10 −7 M −1.sec −1 compared to the blue copper protein which is between 1ms and 01μs. [13] Upon electron transfer the oxidized Cu 2+ state at the blue copper protein active site will be minimized because the Jahn-Teller effect is minimized. The distorted geometry prevents Jahn-Teller ...
Effective concentration (activity) 1 mol/L for each aqueous or amalgamated (mercury-alloyed) species; Unit activity for each solvent and pure solid or liquid species; and Absolute partial pressure 101.325 kPa (1.00000 atm; 1.01325 bar) for each gaseous reagent — the convention in most literature data but not the current standard state (100 kPa).
The trigonal plane of the pyramidal base is composed of two nitrogen atoms (N 1 and N 2) from separate histidines and a sulfur (S 1) from a cysteine. Sulfur (S 2) from an axial methionine forms the apex. The distortion occurs in the bond lengths between the copper and sulfur ligands. The Cu−S 1 contact is shorter (207 pm) than Cu−S 2 (282 pm).
The values below are standard apparent reduction potentials (E°') for electro-biochemical half-reactions measured at 25 °C, 1 atmosphere and a pH of 7 in aqueous solution. [ 1 ] [ 2 ] The actual physiological potential depends on the ratio of the reduced ( Red ) and oxidized ( Ox ) forms according to the Nernst equation and the thermal voltage .
Nitrite reductase EC 1.7.2.1, a 2-domain enzyme containing type-1 and type-2 copper centres. [ 6 ] [ 7 ] In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper.
CCS is a 54kDa protein that is present in mammals and most eukaryotes including yeast. The structure of CCS is composed of three distinct domains that are necessary for its function. [ 6 ] [ 7 ] Although CCS is important for many organisms, there are CCS independent pathways for SOD1, and many species lack CCS all together, such as C. elegans ...
The method combines the reactions of copper ions with the peptide bonds under alkaline conditions (the Biuret test) with the oxidation of aromatic protein residues. The Lowry method is based on the reaction of Cu +, produced by the oxidation of peptide bonds, with Folin–Ciocalteu reagent (a mixture of phosphotungstic acid and phosphomolybdic acid in the Folin–Ciocalteu reaction).