Three substrate binding sites on spinach ferredoxin:NADP+ oxidoreductase. Studies with selectively acting inhibitors

Title:

Three substrate binding sites on spinach ferredoxin:NADP+ oxidoreductase. Studies with selectively acting inhibitors

Creator:

Bojko, M. and Więckowski, S.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:fa71b422-ee8f-4948-a093-656e4164473f
uuid:fa71b422-ee8f-4948-a093-656e4164473f
issn:0300-3604
doi:10.1023/A:1015604128832

Subject:

apoferredoxin, cytochrome c, diaphorase activity, dibromothymoquinone, ferredoxin, and phenylmercuric acetate

Type:

model:article and TEXT

Format:

bez média and svazek

Description:

The effects of phenylmercuric acetate (PMA) and apoferredoxin (apoFd) on the diaphorase activity of spinach ferredoxin:NADP+ oxidoreductase (FNR) in the presence of dibromothymoquinone (DBMIB) or cytochrome c (Cyt c) were studied. PMA inhibited effectively (I50 = < 5 μM) ferredoxin-dependent Cyt c reduction but did not affect evidently the enzyme activity in the presence of DBMIB as an electron acceptor. ApoFd caused also inhibition of Cyt c reduction but slightly stimulated, like ferredoxin, DBMIB reduction. We confirm a hypothesis according to which three binding sites for substrates [NADP(H), Fd-Cyt c, quinone/dichlorophenol indophenol] occur within the molecule of isolated FNR. and M. Bojko, S. Więckowski.

Language:

Multiple languages

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Coverage:

553-556

Source:

Photosynthetica | 2001 Volume:39 | Number:4

Harvested from:

CDK

Metadata only:

false