Abstract
Multicopper oxidases (MCOs) are unique among copper proteins in that they contain at least one each of the three types of biologic copper sites, type 1, type 2, and the binuclear type 3. MCOs are descended from the family of small blue copper proteins (cupredoxins) that likely arose as a complement to the heme-iron-based cytochromes involved in electron transport; this event corresponded to the aerobiosis of the biosphere that resulted in the conversion of Fe(II) to Fe(III) as the predominant redox state of this essential metal and the solubilization of copper from Cu2S to Cu(H2O) n 2+. MCOs are encoded in genomes in all three kingdoms and play essential roles in the physiology of essentially all aerobes. With four redox-active copper centers, MCOs share with terminal copper-heme oxidases the ability to catalyze the four-electron reduction of O2 to two molecules of water. The electron transfers associated with this reaction are both outer and inner sphere in nature and their mechanisms have been fairly well established. A subset of MCO proteins exhibit specificity for Fe2+, Cu+, and/or Mn2+ as reducing substrates and have been designated as metallooxidases. These enzymes, in particular the ferroxidases found in all fungi and metazoans, play critical roles in the metal metabolism of the expressing organism.
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Abbreviations
- Cp:
-
Ceruloplasmin
- hCp:
-
Human ceruloplasmin
- Hp:
-
Hephaestin
- LUMO:
-
Lowest unoccupied molecular orbital
- MCO:
-
Multicopper oxidase
- NiR:
-
Nitrite reductase
- SLAC:
-
Small laccase
- T1:
-
Type 1
- T2:
-
Type 2
- T3:
-
Type 3
- TNC:
-
Trinuclear cluster
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Acknowledgments
The author gratefully acknowledges the several members of his laboratory and his collaborators Edward Solomon and P. John Hart who have together assembled the experimental data that form the basis of our understanding of MCO proteins and their role in metal metabolism. The work in the Kosman laboratory was supported by NIH RO1 DK053820.
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This article will be printed in the upcoming Journal of Biological Inorganic Chemistry special issue Cell Biology of Copper.
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Kosman, D.J. Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology. J Biol Inorg Chem 15, 15–28 (2010). https://doi.org/10.1007/s00775-009-0590-9
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DOI: https://doi.org/10.1007/s00775-009-0590-9