Microgravimetric quartz-crystal microbalance analysis of cytochrome c interactions with pyridine and pyridine-nitrospiropyran monolayer electrodes: Characterization of inter-protein complexes at the functionalized surfaces

Mazzi Lion-Dagan, Iddo Ben-Dov, Itamar Willner*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The association of cytochrome c (Cyt. c) to a pyridine monolayer assembled onto Au electrodes associated with a quartz crystal is followed microgravimetrically using a quartz-crystal microbalance (QCM). The association constant of Cyt. c to the monolayer corresponds to K1 = 8.5 x 103 M-1. The inter-protein binding of cytochrome oxidase (COx) to a pyridine-Cyt. c monolayer assembled on the electrode is similarly characterized by the QCM method. The association constant of COx to Cyt. c is K2 = 1.67 x 106 M-2. A mixed monolayer consisting of pyridine and nitrospiropyran units was assembled on Au electrodes associated with a quartz crystal. The functionalized monolayer was used to photostimulate the association and dissociation of Cyt. c to the monolayer. The system provides a means for the piezoelectric microgravimetric transduction of optical signals recorded by the monolayer-modified surface.

Original languageEnglish
Pages (from-to)251-260
Number of pages10
JournalColloids and Surfaces B: Biointerfaces
Volume8
Issue number4-5
DOIs
StatePublished - 10 Apr 1997

Keywords

  • Cytochrome c
  • Cytochrome oxidase
  • Photoisomerizable monolayer
  • Protein association
  • Quartz crystal microbalance
  • Self-assembled monolayer

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