Enhanced rate of intramolecular electron transfer in an engineered purple CuA azurin
نویسندگان
چکیده
منابع مشابه
An engineered CuA Amicyanin capable of intermolecular electron transfer reactions.
The type I copper center of amicyanin was replaced with a binuclear CuA center. To create this model CuA protein, a portion of the amino acid sequence that contains three of the ligands to the native type I copper center of Paracoccus denitrificans amicyanin was replaced with the corresponding portion of sequence that provides five ligands for the CuA center of cytochrome c oxidase from P. deni...
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Intramolecular electron transfer in azurin in water and deuterium oxide has been studied over a broad temperature range. The kinetic deuterium isotope effect, k(H)/k(D), is smaller than unity (0.7 at 298 K), primarily caused by the different activation entropies in water (-56.5 J K(-1) mol(-1)) and in deuterium oxide (-35.7 J K(-1) mol(-1)). This difference suggests a role for distinct protein ...
متن کاملReversible S-Nitrosylation in an Engineered Azurin
S-Nitrosothiols are known as reagents for NO storage and transportation and as regulators in many physiological processes. Although the S-nitrosylation catalysed by haem proteins is well known, no direct evidence of S-nitrosylation in copper proteins has been reported. Here, we report reversible insertion of NO into a copper-thiolate bond in an engineered copper centre in Pseudomonas aeruginosa...
متن کاملIntramolecular Electron Transfer
In most of the oxidation—reduction reactions involving net electron transfer which have been studied, the experimental results yield only second order rates, and thus reflect the barrier to bringing reactants together as well as that for the electron transfer act itself. Recent advances in synthetic procedures make it possible to measure as an intramolecular or first order process, net electron...
متن کاملElectron transfer reactivity of type zero Pseudomonas aeruginosa azurin.
Type zero copper is a hard-ligand analogue of the classical type 1 or blue site in copper proteins that function as electron transfer (ET) agents in photosynthesis and other biological processes. The EPR spectroscopic features of type zero Cu(II) are very similar to those of blue copper, although lacking the deep blue color, due to the absence of thiolate ligation. We have measured the rates of...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1999
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.96.3.899