• Publications
  • Influence
Structure of a cytochrome P450-redox partner electron-transfer complex.
The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase,Expand
  • 422
  • 29
  • PDF
Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor.
We investigated two male infant patients who were given a diagnosis of progressive mitochondrial encephalomyopathy on the basis of clinical, biochemical, and morphological features. These patientsExpand
  • 150
  • 14
Apoptosis-inducing factor: structure, function, and redox regulation.
  • I. Sevrioukova
  • Biology, Medicine
  • Antioxidants & redox signaling
  • 15 June 2011
Apoptosis-inducing factor (AIF) is a flavin adenine dinucleotide-containing, NADH-dependent oxidoreductase residing in the mitochondrial intermembrane space whose specific enzymatic activity remainsExpand
  • 185
  • 11
Structure and mechanism of the complex between cytochrome P4503A4 and ritonavir
Ritonavir is a HIV protease inhibitor routinely prescribed to HIV patients that also potently inactivates cytochrome P4503A4 (CYP3A4), the major human drug-metabolizing enzyme. By inhibiting CYP3A4,Expand
  • 146
  • 10
  • PDF
Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems.
Cytochromes P450 (CYPs) represent a diverse group of heme-thiolate proteins found in almost all organisms. CYPs share a common protein fold but differ in substrate selectivity and catalyze a wideExpand
  • 82
  • 8
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
Cowchock syndrome (CMTX4) is a slowly progressive X-linked recessive disorder with axonal neuropathy, deafness, and cognitive impairment. The disease locus was previously mapped to an 11 cM region atExpand
  • 97
  • 8
Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation.
X-ray damage to protein crystals is often assessed on the basis of the degradation of diffraction intensity, yet this measure is not sensitive to the rapid changes that occur at photosensitive groupsExpand
  • 77
  • 6
  • PDF
Structural and Mechanistic Insights into the Interaction of Cytochrome P4503A4 with Bromoergocryptine, a Type I Ligand*
Background: Human CYP3A4 metabolizes the majority of administered drugs including bromoergocryptine (BEC), a dopamine receptor agonist. Results: Crystallographic and experimental data suggest theExpand
  • 92
  • 5
Redox-dependent Changes in Molecular Properties of Mitochondrial Apoptosis-inducing Factor*
Mitochondrial apoptosis-inducing factor (AIF) is a central player in the caspase-independent cell death pathway whose normal physiological function remains unclear. Our study showed that naturallyExpand
  • 71
  • 5
Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3.
The flavoprotein domain of P450BM-3 (BMR), which is functionally analogous to eukaryotic NADPH-P450 oxidoreductases, contains both FAD and FMN. When BMR is titrated with NADPH or sodium dithioniteExpand
  • 49
  • 5