The role of cysteine residues of spinach ferredoxin-NADP+ reductase as assessed by site-directed mutagenesis
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00076a010
Reference27 articles.
1. Expression in Escherichia coli of ferredoxin: NADP+ reductase from spinach. Bacterial synthesis of the holoflavoprotein and of an active enzyme form lacking the first 28 amino acid residues of the sequence
2. Identification of Lys116 as the target of N-ethylmaleimide inactivation of ferredoxin:NADP+ oxidoreductase
3. Probing the role of lysine 116 and lysine 244 in the spinach ferredoxin-NADP+ reductase by site-directed mutagenesis.
4. Electron transfer by ferredoxin:NADP+ reductase. Rapid-reaction evidence for participation of a ternary complex.
5. Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties.
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