The Interaction Between Cytochrome f and Plastocyanin or Cytochrome c 6

2016 ◽  
pp. 631-655
Author(s):  
Derek S. Bendall ◽  
Christopher J. Howe
Keyword(s):  
Cytochrome C ◽  
Cytochrome F

Oxyfluorfen and Lipid Peroxidation: Protein Damage as a Phytotoxic Consequence

Weed Science ◽  
1985 ◽  
Vol 33 (6) ◽  
pp. 766-770 ◽  
Author(s):  
Karl J. Kunert ◽  
Carmen Homrighausen ◽  
Herbert Böhme ◽  
Peter Böger
Keyword(s):  
Lipid Peroxidation ◽  
Cytochrome C ◽  
Diphenyl Ether ◽  
Photosynthetic Electron Transport ◽  
Water Soluble ◽  
Cytochrome F ◽  
Protein Damage ◽  
Protein Loss ◽  
Membrane Bound

Protein damage, as a primary phytotoxic consequence of in vivo lipid peroxidation, induced by the diphenyl ether herbicide oxyfluorfen [2-chloro-1-(3-ethoxy-4-nitrophenoxy)-4-(trifluoromethyl)benzene] at a concentration of 10 μM, was measured with the green algaScenedesmus acutus. In the light, water-soluble proteins are destroyed by a herbicide-induced peroxidation process that can be detected by production of fluorescent products and loss of specific amino acid residues of proteins. The water-soluble cytochrome c-553 and the membrane-bound cytochrome f-553, components of the photosynthetic electron transport, were specifically used as sensitive markers for protein damage, measured as decrease of redox reactions of the cytochromes. Under peroxidizing conditions, destruction of the algal cytochrome c is significantly higher than destruction of membrane-bound components, such as cytochrome f and chlorophyll. Protection against protein loss is achieved by the nonbiological antioxidant ethoxyquin (1,2-dihydro-6-ethoxy-2,2,4-trimethylquinoline) or the photosynthesis inhibitor diuron [N′-(3,4-dichlorophenyl)-N,N-dimethylurea].

The Ternary Complex of Cytochrome f and Cytochrome c: Identification of a Second Binding Site and Competition for Plastocyanin Binding

ChemBioChem ◽  
2002 ◽  
Vol 3 (6) ◽  
pp. 526 ◽  
Author(s):  
Peter B. Crowley ◽  
Kersten S. Rabe ◽  
Jonathan A. R. Worrall ◽  
Gerard W. Canters ◽  
Marcellus Ubbink
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Ternary Complex ◽  
Cytochrome F

scholarly journals The purification and amino acid sequence of cytochrome c-552 from Euglena gracilis

1974 ◽  
Vol 139 (2) ◽  
pp. 449-459 ◽  
Author(s):  
G. W. Pettigrew
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Euglena Gracilis ◽  
Cytochrome F ◽  
Evolutionary Significance ◽  
British Library ◽  
Prosthetic Group ◽  
Amino Terminal ◽  
Lending Library

Cytochrome c-552 from Euglena gracilis was purified and the amino acid sequence determined. The protein is a single peptide chain of 87 residues with the haem prosthetic group bound through two thioether linkages to two cysteine residues near the amino-terminal region. The amino acid sequence shows some similarities to mitochondrial cytochrome c and to two prokaryote c-type cytochromes. The sequence, taken with the known characteristics of cytochrome c-552, indicates that it is an f-type cytochrome. The possible functional and evolutionary significance of these features in common is discussed. Detailed evidence for the amino acid sequence of Euglena cytochrome f has been deposited as Supplementary Publication SUP 50027 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7QB, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

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