Literature DB >> 23583818

A three-dimensional printed cell for rapid, low-volume spectroelectrochemistry.

Joseph M Brisendine1, Andrew C Mutter, Jose F Cerda, Ronald L Koder.   

Abstract

We have used three-dimensional (3D) printing technology to create an inexpensive spectroelectrochemical cell insert that fits inside a standard cuvette and can be used with any transmission spectrometer. The cell positions the working, counter, and reference electrodes and has an interior volume of approximately 200 μl while simultaneously providing a full 1-cm path length for spectroscopic measurements. This method reduces the time required to perform a potentiometric titration on a molecule compared with standard chemical titration methods and achieves complete electrolysis of protein samples within minutes. Thus, the device combines the best aspects of thin-layer cells and standard potentiometry.
Copyright © 2013 Elsevier Inc. All rights reserved.

Entities:  

Mesh:

Year:  2013        PMID: 23583818      PMCID: PMC4238967          DOI: 10.1016/j.ab.2013.03.036

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  7 in total

1.  Horse heart cytochrome c. The oxidation-reduction potential and protein structures.

Authors:  Y P Myer; A F Saturno; B C Verma; A Pande
Journal:  J Biol Chem       Date:  1979-11-25       Impact factor: 5.157

2.  Manipulating cofactor binding thermodynamics in an artificial oxygen transport protein.

Authors:  Lei Zhang; J L Ross Anderson; Ismail Ahmed; Jessica A Norman; Christopher Negron; Andrew C Mutter; P Leslie Dutton; Ronald L Koder
Journal:  Biochemistry       Date:  2011-11-08       Impact factor: 3.162

Review 3.  Darwin at the molecular scale: selection and variance in electron tunnelling proteins including cytochrome c oxidase.

Authors:  Christopher C Moser; Christopher C Page; P Leslie Dutton
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2006-08-29       Impact factor: 6.237

4.  Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems.

Authors:  P L Dutton
Journal:  Methods Enzymol       Date:  1978       Impact factor: 1.600

5.  Functionalized de novo designed proteins: mechanism of proton coupling to oxidation/reduction in heme protein maquettes.

Authors:  J M Shifman; C C Moser; W A Kalsbeck; D F Bocian; P L Dutton
Journal:  Biochemistry       Date:  1998-11-24       Impact factor: 3.162

6.  Manipulating Reduction Potentials in an Artificial Safranin Cofactor.

Authors:  Gheevarghese Raju; Joseph Capo; Bruce R Lichtenstein; Jose F Cerda; Ronald L Koder
Journal:  Tetrahedron Lett       Date:  2011-12-14       Impact factor: 2.415

7.  Reversible proton coupled electron transfer in a peptide-incorporated naphthoquinone amino acid.

Authors:  Bruce R Lichtenstein; José F Cerda; Ronald L Koder; P Leslie Dutton
Journal:  Chem Commun (Camb)       Date:  2008-11-25       Impact factor: 6.222

  7 in total
  3 in total

1.  Oxidation-reduction and photophysical properties of isomeric forms of Safranin.

Authors:  Eskil M E Andersen; Hsin Wang; Joshua S H Khoo; Jose F Cerda; Ronald L Koder
Journal:  PLoS One       Date:  2022-06-24       Impact factor: 3.752

2.  A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.

Authors:  Kimberly Rizzolo; Steven E Cohen; Andrew C Weitz; Madeline M López Muñoz; Michael P Hendrich; Catherine L Drennan; Sean J Elliott
Journal:  Nat Commun       Date:  2019-03-07       Impact factor: 14.919

3.  An uncharacteristically low-potential flavin governs the energy landscape of electron bifurcation.

Authors:  Courtney E Wise; Anastasia E Ledinina; David W Mulder; Katherine J Chou; John W Peters; Paul W King; Carolyn E Lubner
Journal:  Proc Natl Acad Sci U S A       Date:  2022-03-15       Impact factor: 12.779

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.