Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Cobalt Proteins, Overview

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_69

Synonyms

Definition

Cobalt is relatively rare among essential trace elements but plays important roles in various living organisms. For instance, cobalamin cofactor comprising a cobalt ion coordinated in a substituted corrin macrocycle is known as vitamin B12, and its deficiency may cause severe damage to mammals. In this entry, the structure and function of vitamin B12-dependent enzymes and non-corrin cobalt enzymes are reviewed.

Introduction

Cobalt is the 27th element in the periodic table and a transition metal with seven d electrons. It can take oxidation states from –I to + IV and preferably exists as Co2+ and Co3+. Cobalt is relatively rare among essential trace elements, and its concentrations in seawater and the cytosol are 10−11 and 10−9 mol dm−3, respectively. Geochemistry of trace metals suggests that the cobalt ion existed in ancient sea in relatively high...

This is a preview of subscription content, log in to check access

References

  1. Besio R, Alleva S, Forlino A et al (2010) Identifying the structure of the active sites of human recombinant prolidase. Eur Biophys J 39:935–945CrossRefPubMedGoogle Scholar
  2. Chai SC, Wang WL, Ye QZ (2008) FE(II) is the native cofactor for Escherichia coli methionine amino peptidase. J Biol Chem 283:26879–26885CrossRefPubMedGoogle Scholar
  3. Das D, Eser BE, Han J et al (2011) Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes. Angew Chem Int Ed Engl 50:7148–7152CrossRefPubMedGoogle Scholar
  4. Escalante-Semerena JC, Warren MJ (2008) Biosynthesis and use of cobalamin (B12). In: Böck A, Curtiss R III, Kaper JB, Karp PD, Neidhardt FC, Nyström T, Slauch JM, Squires CL (eds) EcoSal-Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, DC, Chapter 3.6.3.8Google Scholar
  5. Froese DS, Kochan G, Muniz JRC et al (2010) Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. J Biol Chem 285:38204–38213CrossRefPubMedGoogle Scholar
  6. Ghosh M, Grunden AM, Dunn DM et al (1998) Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 180:4781–4789PubMedGoogle Scholar
  7. Goetzl S, Jeoung J-H, Hennig SE et al (2011) Structural basis for electron and methyl-group transfer in a methyltransferase system operating in the reductive acetyl-CoA pathway. J Mol Biol 411:96–109CrossRefPubMedGoogle Scholar
  8. Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC (2004) Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J 23:3621–3631CrossRefPubMedGoogle Scholar
  9. Hu X, Addlagatta A, Lu J et al (2006) Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc Natl Acad Sci USA 103:18148–18153CrossRefPubMedGoogle Scholar
  10. Itoh N, Kawanami T, Liu JQ (2001) Cloning and biochemical characterization of Co2+-activated bromoperoxidase-esterase (perhydrolase) from Pseudomonas putida IF-3 strain. Biochim Biophys Acta 1545:53–66CrossRefPubMedGoogle Scholar
  11. Kobayashi M, Shimizu S (1999) Cobalt proteins. Eur J Biochem 261:1–9CrossRefPubMedGoogle Scholar
  12. Lowther WT, Matthews BW (2000) Structure and function of the methionine aminopeptidases. Biochim Biophys Acta 1477:157–167CrossRefPubMedGoogle Scholar
  13. Maher MJ, Ghosh M, Grunden AM et al (2004) Structure of the prolidase from Pyrococcus furiosus. Biochemistry 43:2771–2783CrossRefPubMedGoogle Scholar
  14. Matthews RG, Koutmos M, Datta S (2008) Cobalamin- and cobamide-dependent methyltransferases. Curr Opin Struct Biol 18:658–666CrossRefPubMedGoogle Scholar
  15. Oinuma K, Hashimoto Y, Konishi K et al (2003) Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization. J Biol Chem 278:29600–29608CrossRefPubMedGoogle Scholar
  16. Padovani D, Banerjee R (2009) A G-protein editor gates coenzyme B12 loading and is corrupted in methylmalonic aciduria. Proc Natl Acad Sci USA 106:21567–21572CrossRefPubMedGoogle Scholar
  17. Randaccio L, Geremia S, Wuerges J (2007) Crystallography of vitamin B12 proteins. J Organomet Chem 692:1198–1215CrossRefGoogle Scholar
  18. Satchi-Fainaro R, Mamluk R, Wang L et al (2005) Inhibition of vessel permeability by TNP-470 and its polymer conjugate, caplostatin. Cancer Cell 7:251–261CrossRefPubMedGoogle Scholar
  19. Wolthers KR, Scrutton NS (2009) Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase–methionine synthase reductase complex. FEBS J 276:1942–1951CrossRefPubMedGoogle Scholar
  20. Zhu XY, Teng MK, Niu LW et al (2004) Structure of xylose isomerase from Streptomyces diastaticus No. 7 strain M1033 at 1.85 Å resolution. Acta Crystallogr Sect D 56:129–136CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Biotechnology and Life Science, Graduate School of TechnologyTokyo University of Agriculture and TechnologyKoganei, TokyoJapan
  2. 2.Graduate School of Life and Environmental SciencesInstitute of Applied Biochemistry, The University of TsukubaTsukuba, IbarakiJapan