Abstract:
:Compared with algal and cyanobacterial cytochrome c(6), cytochrome c(6A) from higher plants contains an additional loop of 12 amino acid residues. We have determined the first crystal structure of cytochrome c(6A) from Arabidopsis thaliana at 1.5 Angstrom resolution in order to help elucidate its function. The overall structure of cytochrome c(6A) follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys16 and Cys19, and the iron has octahedral coordination with His20 and Met60 as the axial ligands. Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c(6A). Our model provides a chemical basis for the known low redox potential of cytochrome c(6A) which makes it an unsuitable electron carrier between cytochrome b(6)f and PSI.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chida H,Yokoyama T,Kawai F,Nakazawa A,Akazaki H,Takayama Y,Hirano T,Suruga K,Satoh T,Yamada S,Kawachi R,Unzai S,Nishio T,Park SY,Oku Tdoi
10.1016/j.febslet.2006.05.067subject
Has Abstractpub_date
2006-06-26 00:00:00pages
3763-8issue
15eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00684-3journal_volume
580pub_type
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