Premium
A Bioorganometallic Approach to Study Histidine Kinase Autophosphorylations
Author(s) -
Wang Nan,
She Zhe,
Ingar Zakiyya,
Martic Sanela,
Kraatz HeinzBernhard
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201605253
Subject(s) - autophosphorylation , histidine kinase , adenosine triphosphate , histidine , cofactor , kinase , biochemistry , phosphorylation , chemistry , phosphotransferase , biophysics , enzyme , biology , protein kinase a
Auto‐phosphorylation of bacterial histidine kinases PhoR, PhoQ, and EnvZ has been investigated using adenosine‐5′‐[γ‐ferrocene] triphosphate ( Fc‐ATP ) as a cosubstrate for the first time. The study has been carried out in solution and on surface. Results from biochemical multiplex assay and surface electrochemical/optical methods are consistent, which successfully demonstrates that Fc‐ATP is an efficient cosubstrate for histidine kinase auto‐phosphorylations. The study also has discovered that the concentration of Fc‐ATP influences the autophosphorylation efficiency. This developed methodology will provide a powerful tool in studying such biological processes towards further understanding of the involved mechanism.