Nomenclature of Electron-Transfer Proteins

The recommendations in this version are identical to the document published in Enzyme Nomenclature Academic Press, San Diego, California, 1992, pp. 534-561; Biochim. Biophys. Acta, 1991, 1060, between page 236 and 237 (retains original EJB page numbers); Eur. J. Biochem., 1991, 200, 599-611 (correction 1993, 213, 2-3); J. Biol. Chem., 1992, 267, 665-677. [Copyright IUBMB]. If you need to quote this document please cite these references.Any comments, corrections or suggestions for a future edition should be e-mailed to g.p.moss@qmul.ac.uk (Dr G P Moss) or other member of the Committees. In the web version an error in the Enzyme Nomenclature version has been corrected and marked by , which is a link to details of the change and where it applies. The error list also details errors in the three journal versions.

All footnotes in the printed versions have been converted into notes following the relevant paragraph.

The last two editions of Enzyme Nomenclature have included an appendix on the nomenclature of electron-transfer proteins. The Nomenclature Committee of the International Union of Biochemistry decided in 1984 that this needed substantial revision, and set up a panel whose original members were: H. Beinert, R.C. Bray, C.C. Greenwood, V. Massey, E. Münck, G. Palmer, (convenor), J. Peisach, E.C. Slater, B.E. Smith and D.M. Ziegler.

Since that time the panel has been assisted by S.P.J. Albracht, B.A. Averill, R.P. Ambler, G.W. Canters, M. Cusanovich, J.A. Duine, H.C. Freeman, G.J. Leigh, T. Meyer, A.G. Sykes, R. Timkovich, R. Wever, P.M. Wood and T. Yamanaka. The first draft of these recommendations was prepared by Graham Palmer, Rice University, Houston, Texas, U.S.A. After approval by NC-IUB in 1989 the recommendations were extended and prepared for publication by Jan Reedijk, Leiden University, The Netherlands.

Contents

• 1. General Introduction
• 2. Flavoproteins
• 3. Proteins Containing Reducible Disulfide
• 4. Cytochromes
  • 4.1 Introduction and definitions
  • 4.2. Cytochrome Groups
  • 4.3 Variability in Cytochrome Groups
  • 4.4 List of Cytochromes
    • 4.4.1 Cytochrome a group
    • 4.4.2 Cytochrome b group
    • 4.4.3 Cytochrome c group
    • 4.4.4 Cytochrome d group
• 5. Non-Heme Iron Proteins
  • 5.1 Introduction
  • 5.2 Types of simple iron-sulfur protein
    • 5.2.1 Rubredoxins
    • 5.2.2 Ferredoxins
    • 5.2.3 Other iron-sulfur proteins
  • 5.3 Recommendations for designating iron-sulfur proteins
    • 5.3.1 General recommendations
    • 5.3.2 Designation of clusters
    • 5.3.3 Examples
    • 5.3.4 Clusters of different types
  • 5.4 Other iron proteins
• 6. Copper Proteins
  • 6.1 Type 1 Copper Proteins
  • 6.2 Type 2 Copper Proteins
  • 6.3 Type 3 Copper Proteins
  • 6.4 Multi-Copper Oxidases
  • 6.5 Copper Centres in Cytochrome Oxidase
• 7. Molybdenum Proteins
  • 7.1 Molybdenum enzymes (general)
  • 7.2 Additional centres
  • 7.3 Molybdenum enzymes containing the iron-molybdenum cofactor
  • 7.4 Molybdenum enzymes containing the pterin-molybdenum cofactor
  • 7.5 Other molybdenum enzymes
• 8. Nickel Proteins
• 9. Vanadium Proteins
• 10. Quinoproteins
• 11. Metal-Substituted Metalloproteins
• 12. References