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 Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase.

1978 ◽  
Vol 253 (10) ◽  
pp. 3730-3735
Author(s):  
T.L. Poulos ◽  
S.T. Freer ◽  
R.A. Alden ◽  
N.H. Xuong ◽  
S.L. Edwards ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Cyanide Binding

scholarly journals Probing the oxygen binding site of cytochrome c oxidase by cyanide.

1994 ◽  
Vol 269 (39) ◽  
pp. 24114-24119
Author(s):  
M.T. Wilson ◽  
G. Antonini ◽  
F. Malatesta ◽  
P. Sarti ◽  
M. Brunori
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Oxidase ◽  
Oxygen Binding

WHERE IS THE MITOCHONDRIAL BINDING SITE FOR CYTOCHROME c?

1971 ◽  
pp. 431-436 ◽  
Author(s):  
Peter Nicholls ◽  
Harold Kimelberg ◽  
Eugene Mochan ◽  
Bonnie S. Mochan ◽  
W.B. Elliott
Keyword(s):  
Cytochrome C ◽  
Binding Site

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].

scholarly journals New Ligands of the Conserved Steroid Binding Site of Cytochrome c Oxidase

2012 ◽  
Vol 102 (3) ◽  
pp. 574a ◽  
Author(s):  
Carrie Hiser ◽  
Leann Buhrow ◽  
Jian Liu ◽  
Shelagh Ferguson-Miller
Keyword(s):  
Cytochrome C ◽  
Binding Site ◽  
Cytochrome C Oxidase ◽  
Steroid Binding

scholarly journals The nucleotide sequence and deduced amino acid sequence of the cytochrome cL gene of Methylobacterium extorquens AM1, a novel class of c-type cytochrome

1988 ◽  
Vol 256 (2) ◽  
pp. 673-676 ◽  
Author(s):  
D N Nunn ◽  
C Anthony
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Methylobacterium Extorquens ◽  
Methylobacterium Extorquens Am1 ◽  
Cytochrome Cl

The nucleotide sequence and deduced amino acid sequence of the cytochrome cL of Methylobacterium extorquens (Pseudomonas AM1; Methylobacterium AM1) shows that this cytochrome c is completely different, except for its haem-binding site, from all other cytochromes.

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