Effector proteins from P450cam and methane monooxygenase: Lessons in tuning nature's powerful reagents

Brian J. Brazeau, Bradley J. Wallar, John D. Lipscomb

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Effector proteins alter the kinetic or catalytic course of many oxygenase reactions. One of the first oxygenase effectors to be described was putidaredoxin, which serves to gate electron transfer into oxy-P450 cam. In the nonheme, methane monooxygenase (MMO) system, the B-component (MMOB) serves a distinct effector function by gating substrate and oxygen into the active site of the hydroxylase component (MMOH). Here the binding parameters and binding surfaces of the MMOB-MMOH complex are determined by site-specific labeling, fluorescence titrations, chemical cross-linking, and MALDI-TOF peptide identification. Based on these data, a model for the bimolecular complex is described and a hypothesis for the structural basis for the effector function is elaborated. The bearing on the putidaredoxin effector function is discussed.

Original languageEnglish (US)
Pages (from-to)143-148
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume312
Issue number1
DOIs
StatePublished - Dec 5 2003

Keywords

  • Component docking
  • Cross-linking
  • Effector
  • Fluorescence
  • Kinetics
  • Methane monooxygenase
  • P450
  • Regulation

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