Literature DB >> 23859602

Electron flow through nitrotyrosinate in Pseudomonas aeruginosa azurin.

Jeffrey J Warren1, Nadia Herrera, Michael G Hill, Jay R Winkler, Harry B Gray.   

Abstract

We have designed ruthenium-modified Pseudomonas aeruginosa azurins that incorporate 3-nitrotyrosine (NO2YOH) between Ru(2,2'-bipyridine)2(imidazole)(histidine) and Cu redox centers in electron transfer (ET) pathways. We investigated the structures and reactivities of three different systems: RuH107NO2YOH109, RuH124NO2YOH122, and RuH126NO2YOH122. RuH107NO2YOH109, unlabeled H124NO2YOH122, and unlabeled H126NO2YOH122 were structurally characterized. The pKa's of NO2YOH at positions 122 and 109 are 7.2 and 6.0, respectively. Reduction potentials of 3-nitrotyrosinate (NO2YO(-))-modified azurins were estimated from cyclic and differential pulse voltammetry data: oxidation of NO2YO(-)122 occurs near 1.1 versus NHE; oxidation of NO2YO(-)109 is near 1.2 V. Our analysis of transient optical spectroscopic experiments indicates that hopping via NO2YO(-) enhances Cu(I) oxidation rates over single-step ET by factors of 32 (RuH107NO2YO(-)109), 46 (RuH126NO2YO(-)122), and 13 (RuH124NO2YO(-)122).

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Year:  2013        PMID： 23859602      PMCID： PMC3839300          DOI： 10.1021/ja403734n

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


  42 in total

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5.  Site-specific incorporation of 3-nitrotyrosine as a probe of pKa perturbation of redox-active tyrosines in ribonucleotide reductase.

Authors:  Kenichi Yokoyama; Ulla Uhlin; Joanne Stubbe
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6.  Electron hopping through proteins.

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  18 in total

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Review 7.  Mechanisms for control of biological electron transfer reactions.

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8.  Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.

Authors:  Jeffrey J Warren; Oliver S Shafaat; Jay R Winkler; Harry B Gray
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9.  Driving Protein Conformational Changes with Light: Photoinduced Structural Rearrangement in a Heterobimetallic Oxidase.

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