Cytochromes b561

Ascorbate-mediated trans-membrane electron transport

Han Asard, Raffaella Barbaro, Paolo Trost, A. Bérczi

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Significance: Cytochromes b561 (CYB561s) constitute a family of trans-membrane (TM), di-heme proteins, occurring in a variety of organs and cell types, in plants and animals, and using ascorbate (ASC) as an electron donor. CYB561s function as monodehydroascorbate reductase, regenerating ASC, and as Fe3+-reductases, providing reduced iron for TM transport. A CYB561-core domain is also associated with dopamine β-monooxygenase redox domains (DOMON) in ubiquitous CYBDOM proteins. In plants, CYBDOMs form large protein families. Physiological functions supported by CYB561s and CYBDOMs include stress defense, cell wall modifications, iron metabolism, tumor suppression, and various neurological processes, including memory retention. CYB561s, therefore, significantly broaden our view on the physiological roles of ASC. Recent Advances: The ubiquitous nature of CYB561s is only recently being recognized. Significant advances have been made through the study of recombinant CYB561s, revealing structural and functional properties of a unique "two-heme four-helix" protein configuration. In addition, the DOMON domains of CYBDOMs are suggested to contain another heme b. Critical Issues: New CYB561 proteins are still being identified, and there is a need to provide an insight and overview on the various roles of these proteins and their structural properties. Future Directions: Mutant studies will reveal in greater detail the mechanisms by which CYB561s and CYBDOMs participate in cell metabolism in plants and animals. Moreover, the availability of efficient heterologous expression systems should allow protein crystallization, more detailed (atomic-level) structural information, and insights into the intra-molecular mechanism of electron transport.

Original languageEnglish
Pages (from-to)1026-1035
Number of pages10
JournalAntioxidants and Redox Signaling
Volume19
Issue number9
DOIs
Publication statusPublished - Sep 20 2013

Fingerprint

Electron Transport
Membranes
Proteins
Mixed Function Oxygenases
Heme
Metabolism
Oxidation-Reduction
Dopamine
Oxidoreductases
Animals
Iron
Hemeproteins
Plant Cells
Crystallization
Cell Wall
cytochrome b561
Structural properties
Tumors
Cells
Availability

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Physiology
  • Clinical Biochemistry

Cite this

Cytochromes b561 : Ascorbate-mediated trans-membrane electron transport. / Asard, Han; Barbaro, Raffaella; Trost, Paolo; Bérczi, A.

In: Antioxidants and Redox Signaling, Vol. 19, No. 9, 20.09.2013, p. 1026-1035.

Research output: Contribution to journalArticle

Asard, Han ; Barbaro, Raffaella ; Trost, Paolo ; Bérczi, A. / Cytochromes b561 : Ascorbate-mediated trans-membrane electron transport. In: Antioxidants and Redox Signaling. 2013 ; Vol. 19, No. 9. pp. 1026-1035.
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