Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering

Chem Commun (Camb). 2011 Jan 7;47(1):289-91. doi: 10.1039/c0cc01817a. Epub 2010 Aug 24.

Abstract

Here we report structural dynamics of equine myoglobin (Mb) in response to the CO photodissociation visualized by picosecond time-resolved X-ray solution scattering. The data clearly reveal new structural dynamics that occur in the timescale of ∼360 picoseconds (ps) and ∼9 nanoseconds (ns), which have not been clearly detected in previous studies.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Monoxide / chemistry
  • Myoglobin / chemistry*
  • Photochemistry
  • Protein Conformation
  • Scattering, Small Angle
  • Solutions
  • Thermodynamics*
  • Time Factors
  • X-Ray Diffraction

Substances

  • Myoglobin
  • Solutions
  • Carbon Monoxide