Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship As Studied by Site-Directed Mutagenesis and X-ray Crystallography-Reference-Cited by-同舟云学术

Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship As Studied by Site-Directed Mutagenesis and X-ray Crystallography

Published:1995-07-04 Issue:26 Volume:34 Page:8371-8379
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Aliverti Alessandro,Bruns Christopher M.,Pandini Vittorio E.,Karplus P. Andrew,Vanoni Maria A.,Curti Bruno,Zanetti Giuliana

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00026a019

Reference26 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. Probing the role of lysine 116 and lysine 244 in the spinach ferredoxin-NADP+ reductase by site-directed mutagenesis.

3. The role of cysteine residues of spinach ferredoxin-NADP+ reductase as assessed by site-directed mutagenesis

4. Involvement of lysine-88 of spinach ferredoxin-NADP+reductase in the interaction with ferredoxin

5. Electron transfer by ferredoxin:NADP+ reductase. Rapid-reaction evidence for participation of a ternary complex.

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