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Literature DB >> 8516286

Electron self-exchange in azurin: calculation of the superexchange electron tunneling rate.

K V Mikkelsen¹, L K Skov, H Nar, O Farver.

Abstract

Electronic coupling between the copper atoms in an azurin dimer has been calculated in this conformationally well-defined system by using many-electronic wave functions. When one of the two water molecules forming intermolecular hydrogen bonds between the copper-ligating His-117 of the two azurins is removed, the calculated coupling element is reduced from 2.5 x 10(-6) to 1.1 x 10(-7) eV (1 eV = 1.602 x 10(-19) J). Also, the effects of the relative orientations of the two water molecules have been analyzed. The results show that water molecules may play an important role as switches for biological electron transfer. The rate of electron self-exchange between two azurins has been calculated, and the result is in very good agreement with the rate found experimentally.

Entities: Chemical

Mesh：

Substances：
Azurin

Year: 1993 PMID： 8516286 PMCID： PMC46736 DOI： 10.1073/pnas.90.12.5443

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

11 in total

Review 1. Pathway analysis of protein electron-transfer reactions.

Authors: J N Onuchic; D N Beratan; J R Winkler; H B Gray
Journal: Annu Rev Biophys Biomol Struct Date: 1992

2. [Brachial vein thrombosis].

Authors: J Kaczynski; O Larsson
Journal: Lakartidningen Date: 1981-11-04

3. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa.

Authors: H Nar; A Messerschmidt; R Huber; M van de Kamp; G W Canters
Journal: J Mol Biol Date: 1991-03-20 Impact factor: 5.469

4. The effect of driving force on intramolecular electron transfer in proteins. Studies on single-site mutated azurins.

Authors: O Farver; L K Skov; M van de Kamp; G W Canters; I Pecht
Journal: Eur J Biochem Date: 1992-12-01

5. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip.

Authors: H Nar; A Messerschmidt; R Huber; M van de Kamp; G W Canters
Journal: J Mol Biol Date: 1991-10-05 Impact factor: 5.469

6. Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa.

Authors: M van de Kamp; G W Canters; S S Wijmenga; A Lommen; C W Hilbers; H Nar; A Messerschmidt; R Huber
Journal: Biochemistry Date: 1992-10-27 Impact factor: 3.162

7. Structure of azurin from Alcaligenes denitrificans refinement at 1.8 A resolution and comparison of the two crystallographically independent molecules.

Authors: E N Baker
Journal: J Mol Biol Date: 1988-10-20 Impact factor: 5.469

8. Preparation and characterization of pentaammineruthenium-(histidine-83)azurin: thermodynamics of intramolecular electron transfer from ruthenium to copper.

Authors: R Margalit; N M Kostić; C M Che; D F Blair; H J Chiang; I Pecht; J B Shelton; J R Shelton; W A Schroeder; H B Gray
Journal: Proc Natl Acad Sci U S A Date: 1984-10 Impact factor: 11.205

9. 1H nuclear magnetic resonance study of the protonation behaviour of the histidine residues and the electron self-exchange reaction of azurin from Alcaligenes denitrificans.

Authors: C M Groeneveld; M C Ouwerling; C Erkelens; G W Canters
Journal: J Mol Biol Date: 1988-03-05 Impact factor: 5.469