Complex formation between flavodoxin and cytochrome c. Cross-linking studies

Autor:	J L, Dickerson, J J, Kornuc, D C, Rees
Rok vydání:	1985
Předmět:	Flavoproteins Protein Conformation Azotobacter Osmolar Concentration Flavodoxin Cytochrome c Group Electrophoresis Polyacrylamide Gel Mathematics
Zdroj:	The Journal of biological chemistry. 260(8)
ISSN:	0021-9258 6366-6375
Popis:	Complex formation between Azotobacter vinelandii flavodoxin and horse cytochrome c has been demonstrated through cross-linking studies with dimethyl suberimidate, dimethyl adipimidate, 1-ethyl-3-(3-di-methylaminopropyl)carbodiimide, and dimethyl-3,3'-dithiobispropionimidate. Essentially quantitative cross-linking of cytochrome c and flavodoxin was observed at low ionic strengths with the carbodiimide cross-linking reagent. An association constant of 4 X 10(4) M-1 was obtained between cytochrome c and flavodoxin at 88 mM ionic strength from analysis of the cross-linking studies. This value is similar to the association constant determined kinetically during the electron transfer reaction between cytochrome c and flavodoxin (Simondsen, R.P., Weber, P.C., Salemme, F.R., and Tollin, G. (1982) Biochemistry 21, 6366-6375), and suggests that the cross-linked complex may be similar to the precursor complex identified kinetically. A structural model for the flavodoxin-cytochrome c complex proposed by these workers is shown to be compatible with the present cross-linking results.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::90f32eb0a8cef50bb47699f152f6376b https://pubmed.ncbi.nlm.nih.gov/2985577 Zobrazit plný text záznamu