• Publications
  • Influence
Flavohemoglobin and nitric oxide detoxification in the human protozoan parasite Giardia intestinalis.
Flavohemoglobins (flavoHbs), commonly found in bacteria and fungi, afford protection from nitrosative stress by degrading nitric oxide (NO) to nitrate. Giardia intestinalis, a microaerophilicExpand
  • 45
  • 5
Trichomonas vaginalis degrades nitric oxide and expresses a flavorubredoxin-like protein: a new pathogenic mechanism?
Besides possessing many physiological roles, nitric oxide (NO) produced by the immune system in infectious diseases has antimicrobial effects. Trichomoniasis, the most widespread non-viral sexuallyExpand
  • 42
  • 3
The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth
Hydrogen sulfide (H2S) impairs mitochondrial respiration by potently inhibiting the heme-copper cytochrome c oxidase. Since many prokaryotes, including Escherichia (E.) coli, generate H2S andExpand
  • 51
  • 2
  • PDF
Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress
Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b 558, b 595 and d. We found that the enzyme, as‐prepared or in turnover with O2, rapidly decomposes H2O2 with formation ofExpand
  • 49
  • PDF
Cytochrome bd Oxidase and Hydrogen Peroxide Resistance in Mycobacterium tuberculosis
Cytochrome bd oxidase is a prokaryotic respiratory oxidase, phylogenetically unrelated to the well-known heme-copper oxidases, which catalyzes the reduction of O2 to 2H2O. Apart from having a role inExpand
  • 21
How bacteria breathe in hydrogen sulfide-rich environments
Hydrogen sulfide (H2S) is now universally recognized as an endogenous signalling molecule playing a central role in human physiology. This gas, although it controls a number of physiologicalExpand
  • 7
  • PDF
Control of Electron Transfer to the Binuclear Center in Cu-Heme Oxidases
Figure 1 depicts the structure of the active site of cytochrome c oxidase, including cytochrome a and the (oxygen binding) binuclear center cytochrome a 3-CuB as obtained from the crystallographicExpand