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Hydrogen bond network of cytochrome P-450cam: a network connecting the heme group with helix K

K Yoshikawa1, T Noguti, M Tsujimura

  • 1Department of Biology, Faculty of Science, Nagoya University, Japan.

Biochimica Et Biophysica Acta
|July 13, 1992
PubMed

Insights

A mutant P-450cam protein with a lysine substitution at Glu-286 showed a disrupted hydrogen bond network. This structural change likely causes the heme group to be improperly positioned in the enzyme.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Cytochrome P-450 enzymes (P-450cam) are crucial for catalyzing oxidation reactions.
  • The structural integrity of P-450cam is essential for its catalytic function and heme group binding.
  • Hydrogen bonding networks play a significant role in protein structure and stability.

Purpose of the Study:

  • To investigate the structural consequences of a specific mutation in P-450cam (Glu-286 to lysine).
  • To elucidate the role of the hydrogen bond network involving helices K and L in heme group positioning.

Main Methods:

  • Structural characterization of a mutant P-450cam protein.
  • Analysis of hydrogen bonding interactions between protein structures and the heme group.

Main Results:

  • Evidence of a hydrogen bond network connecting helix K to the heme group via helix L was identified.
  • The Glu-286 to lysine mutation in P-450cam resulted in a loss of proper heme group positioning.
  • The disruption of the identified hydrogen bond network is implicated in the observed instability of the heme group.

Conclusions:

  • The study reveals a critical hydrogen bond network essential for maintaining the P-450cam heme group's structural integrity.
  • Mutation of Glu-286 to lysine disrupts this network, leading to functional impairment.
  • Understanding these structural-functional relationships is vital for P-450 enzyme engineering and drug design.

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