Redox properties of Cys₂His₂ and Cys₄ zinc fingers determined by electrospray ionization mass spectrometry.

ABSTRACT: Zinc finger (ZF) protein motifs, stabilized by binding of Zn(II), typically function as interaction modules that bind nucleic acids, proteins and other molecules. The elucidation of the redox states of ZF proteins in cellular conditions, which depend on their midpoint redox potentials, is important for understanding of ZF functioning. In the present study we determined the midpoint redox potentials for representatives of Cys₂His₂ and Cys₄ types of ZF proteins in apo and Zn(II)-bound forms using electrospray ionization mass spectrometry. The midpoint redox potentials of the apo forms of Cys₂His₂ and Cys₄ ZF proteins were -326 and -365 mV (pH 7.5), respectively. These values are close to the cytosolic redox potential of approx

SUBMITTER: Smirnova J 

PROVIDER: S-EPMC5985984 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature