Department of Biology

Aarhus University Seal / Aarhus Universitets segl

Elin Ellebæk Petersen

The Zebrafish Cytochrome b(5)/Cytochrome b(5) Reductase/NADH System Efficiently Reduces Cytoglobins 1 and 2: Conserved Activity of Cytochrome b(5)/Cytochrome b(5) Reductases during Vertebrate Evolution

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Matthew B. Amdahl, University of Pittsburgh
  • ,
  • Elin E. Petersen
  • Kaitlin Bocian, University of Pittsburgh
  • ,
  • Stefan J. Kaliszuk, University of Pittsburgh
  • ,
  • Anthony W. DeMartino, University of Pittsburgh
  • ,
  • Sagarika Tiwari, University of Pittsburgh
  • ,
  • Courtney E. Sparacino-Watkins, University of Pittsburgh
  • ,
  • Paola Corti, University of Pittsburgh
  • ,
  • Jason J. Rose, University of Pittsburgh
  • ,
  • Mark T. Gladwin, University of Pittsburgh
  • ,
  • Angela Fago
  • Jesus Tejero, University of Pittsburgh

Cytoglobin is a heme protein evolutionarily related to hemoglobin and myoglobin. Cytoglobin is expressed ubiquitously in mammalian tissues; however, its physiological functions are yet unclear. Phylogenetic analyses indicate that the cytoglobin gene is highly conserved in vertebrate clades, from fish to reptiles, amphibians, birds, and mammals. Most proposed roles for cytoglobin require the maintenance of a pool of reduced cytoglobin (Fe-II). We have shown previously that the human cytochrome b(5)/cytochrome b(5) reductase system, considered a quintessential hemoglobin/myoglobin reductant, can reduce human and zebrafish cytoglobins

Original languageEnglish
JournalBiochemistry
Volume58
Issue29
Pages (from-to)3212-3223
Number of pages12
ISSN0006-2960
DOIs
Publication statusPublished - Jul 2019

    Research areas

  • NITRIC-OXIDE, REDUCTION POTENTIALS, HUMAN NEUROGLOBIN, B5 REDUCTASE, GLOBIN, METHEMOGLOBIN, MITOCHONDRIAL, MEMBRANE, BINDING, MECHANISMS

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