Skip to main content
SpringerLink
Log in

Resolution, Characterisation and Classification of c-Type Cytochromes

  • Chapter
Cytochromes c

Part of the book series: Springer Series in Molecular Biology ((SSMOL))

Abstract

Functional studies of cytochromes fall into one of two groups. In the first, the intact respiratory system is examined using methods which allow the resolution of individual components. In the second, components are isolated and characterised and their role studied in reconstituted partial systems. Relatively few studies incorporate both approaches and we suggest that this has led to problems in the interpretation of results.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Almassy RJ, Dickerson RE (1978) Pseudomonas cytochrome c-551 at 2.0 Å resolution: enlargement of the cytochrome c family. Proc Natl Acad Sci USA 75:2674–2678

    Article  PubMed  CAS  Google Scholar 

  • Ambler RP (1977) Amino acid sequences and bacterial phylogeny. In: Matsubara H, Yamanaka T (eds) Evolution of protein molecules. Univ Tokyo Press

    Google Scholar 

  • Ambler RP (1980) The structure and classification of cytochromes c. In: Robinson AB, Kaplan NO (eds) From cyclotrons to cytochromes. Academic Press, London New York, pp 263–279

    Google Scholar 

  • Ambler RP, Meyer TE, Kamen MD (1979a) Anomalies in amino acid sequences of small cytochromes c and cytochromes c’ from two species of purple photosynthetic bacteria. Nature (London) 278:661–662

    Article  CAS  Google Scholar 

  • Ambler RP, Daniel M, Hermoso J, Meyer TE, Bartsch RG, Kamen MD (1979b) Cytochrome c2 sequence variation among the recognised species of purple non-sulfur photosynthetic bacteria. Nature (London) 278:559–560

    Google Scholar 

  • Ambler RP, Daniel M, Mellis K, Stout CD (1984) The amino acid sequence of the diheme cytochrome c4 from Azotobacter vinelandii. Biochem J 222:217–227

    PubMed  CAS  Google Scholar 

  • Barrett J (1956) The prosthetic group of cytochrome a2. Biochem J 64:626–639

    PubMed  CAS  Google Scholar 

  • Bartsch RG (1971) Bacterial cytochromes. In: San Pietro A (ed) Methods in enzymology, photosynthesis, part A. Academic Press, London New York, pp 344–363

    Chapter  Google Scholar 

  • Caughey WS, Smythe GA, O’Keefe DH, Maskasy JE, Smith ML (1975) Heme A of cytochrome oxidase — structure and properties — comparisons with hemes B, C and S and derivatives. J Biol Chem 250:7602–7612

    PubMed  CAS  Google Scholar 

  • Chang CK (1985) On the structure of heme d1. J Biol Chem 260:9520–9522

    PubMed  CAS  Google Scholar 

  • Dickerson RE (1980) Cytochrome c and the evolution of energy metabolism. Sci Am 242, 3:98–109

    Article  Google Scholar 

  • Falk JE (1964) Porphyrins and metalloporphyrins. Elsevier, Amsterdam

    Google Scholar 

  • Ferguson-Miller S, Brautigan DL, Margoliash E (1978) Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase. J Biol Chem 251:1104–1115

    Google Scholar 

  • Fiechtner MD, Kassner RJ (1979) Redox properties and heme environment of cytochrome c-551.5 from Desulfuromonas acetoxidans. Biochim Biophys Acta 579:269–278

    PubMed  CAS  Google Scholar 

  • Goodhew C, Brown K, Pettigrew GW (1986) Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochim Biophys Acta 852:288–294

    Article  CAS  Google Scholar 

  • Goodwin TW, Morton RA (1946) The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem J 40:628–632

    CAS  Google Scholar 

  • Haser R, Pierrot M, Frey M, Payan F, Astier JP, Bruschi M, Le-Gall J (1979) Structure and sequence of the multiheme cytochromes c3. Nature (London) 282:806–810

    Article  CAS  Google Scholar 

  • Hon-nami K, Oshima T (1980) Cytochrome oxidase from an extreme thermophile, Thermus thermophilus HB 8. Biochem Biophys Res Commun 92:1023–1029

    Article  CAS  Google Scholar 

  • Jacobs AJ, Kaha VK, Cavari B, Brodie AF (1979) Purification, physicochemical properties and localisation of cytochrome c in energy transducing membranes from Mycobacterium phlei. Arch Biochem Biophys 194:531–541

    Article  PubMed  CAS  Google Scholar 

  • Korszun ZR, Salemme FR (1977) Structure of cytochrome c-555 from Chlorobium thiosulfatophilum: primitive low-potential cytochrome c. Proc Natl Acad Sci USA 74:5244–5247

    Article  PubMed  CAS  Google Scholar 

  • Lemberg R, Barrett J (1973) The cytochromes. Academic Press, London New York

    Google Scholar 

  • Meyer TE (1970) Comparative studies on soluble iron containing proteins in photosynthetic bacteria. PhD thesis, Univ Cal

    Google Scholar 

  • Meyer TE, Kamen MD (1982) New perspectives on c-type cytochromes. Adv Protein Chem 35:105–212

    Article  PubMed  CAS  Google Scholar 

  • Meyer TE, Bartsch RG, Kamen MD (1971) Cytochrome c3 — a class of electron transfer proteins found in both photosynthetic and sulfate reducing bacteria. Biochim Biophys Acta 245:453–464

    Article  PubMed  CAS  Google Scholar 

  • Parr SR, Wilson MT, Greenwood C (1974) The reaction of Pseudomonas aeruginosa cytochrome c oxidase with sodium metabisulfite. Biochem J 139:273–276

    PubMed  CAS  Google Scholar 

  • Penke B, Ferenczi R, Kovacs K (1974) A new acid hydrolysis method for determining tryptophan in peptides and proteins. Anal Biochem 60:45–50

    Article  PubMed  CAS  Google Scholar 

  • Pettigrew GW, Leaver JL, Meyer TE, Ryle AP (1975) Purification, properties and amino acid sequence of atypical cytochrome c from two Protozoa Euglena gracilis and Crithidia oncopelti. Biochem J 147:291–302

    PubMed  CAS  Google Scholar 

  • Shioi Y, Takamiya K, Nishimura M (1972) Studies on energy and electron transfer systems in the green photosynthetic bacterium, “Chloropseudomonas 2K”. J Biochem 71:285–291

    PubMed  CAS  Google Scholar 

  • Smith L, Nava ME, Margoliash E (1973) In: King TE, Mason HS, Morrison M (eds) Oxidases and related redox systems, vol. 2. Univ Park Press, Baltimore, pp 629–638

    Google Scholar 

  • Thomas PE, Ryan D, Levin W (1976) An improved staining procedure for the detection of the peroxidase activity of cytochrome P450 on sodium dodecyl sulfate Polyacrylamide gels. Anal Biochem 75:168–176

    Article  PubMed  CAS  Google Scholar 

  • Thompson M, Barrett J, McDonald E, Battersby AR, Fookes CJR, Chaudhry IA, Clezy PS, Morris HR (1977) Cytochrome c oxidase — isolation, crystallisation and synthesis of porphyrin A-dimethylester. J Chem Soc Chem Commun 278–279

    Google Scholar 

  • Timkovich R, Cork MS, Taylor PV (1984) Proposed structure for the non-covalently associated heme prosthetic group of dissimilatory nitrite reductases. J Biol Chem 259:15089–15093

    PubMed  CAS  Google Scholar 

  • Weber PC, Bartsch RG, Cusanovich MA, Hamlin RC, Howard A, Jordan SR, Kamen MD, Meyer TE, Weatherford DW, Xuong NH, Salemme FR (1980) Structure of cytochrome c’: a dimeric high-spin heme protein. Nature (London) 286:302–305

    Article  CAS  Google Scholar 

  • Wood PM (1980) Interrelationships of the two c-type cytochromes in Rhodopseudomonas sphaeroides photosynthesis. Biochem J 192:761–764

    PubMed  CAS  Google Scholar 

  • Wood PM (1981) Fluorescent gels as a general technique for characterising bacterial c-type cytochromes. Anal Biochem 111:235–239

    Article  PubMed  CAS  Google Scholar 

  • Wood PM (1983) Why do c-type cytochromes exist? FEBS Lett 164:223–226

    Article  PubMed  CAS  Google Scholar 

  • Yamanaka T (1972) Evolution of the cytochrome c molecule. Adv Biophys 3:229–276

    Google Scholar 

  • Yamanaka T (1975) A comparative study on the redox reactions of cytochromes c with certain enzymes. J Biochem 77:493–499

    CAS  Google Scholar 

  • Yamanaka T, Okunuki K (1968) Comparative studies on reactivities of cytochrome c with cytochrome oxidases. In: Okunuki K, Sekuzu I, Kamen MD (eds) Structure and function of cytochromes. Univ Park Press, Baltimore, pp 390–403

    Google Scholar 

  • Yamanaka T, Okunuki K (1974) Cytochromes. In: Microbial iron metabolism. Academic Press, London New York

    Google Scholar 

  • Yu CA, Yu L, King TE (1974) Soluble cytochrome bc1 complex and the reconstitution of succinate cytochrome c reductase. J Biol Chem 249:4905–4910

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Royal (Dick) School of Veterinary Studies, Summerhall, EH9 1QH, Edinburgh, UK

    Dr. Graham W. Pettigrew

  2. School of Chemical Sciences, University of East Anglia, NR4 7TJ, Norwich, UK

    Dr. Geoffrey R. Moore

Authors
  1. Dr. Graham W. Pettigrew
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Dr. Geoffrey R. Moore
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1987 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Pettigrew, G.W., Moore, G.R. (1987). Resolution, Characterisation and Classification of c-Type Cytochromes. In: Cytochromes c. Springer Series in Molecular Biology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-72698-9_1

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-72698-9_1

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-72700-9

  • Online ISBN: 978-3-642-72698-9

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation