X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP+ Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa,-Reference-Cited by-同舟云学术

X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP+ Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa,

Published:2008-07-08 Issue:31 Volume:47 Page:8080-8093
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang An¹,Rodríguez Juan Carlos¹,Han Huijong¹,Schönbrunn Ernst¹,Rivera Mario¹

Affiliation:

1. Ralph N. Adams Institute for Bioanalytical Chemistry and Department of Chemistry, University of Kansas, Multidisciplinary Research Building, 2030 Becker Drive, Room 220 E, Lawrence, Kansas 66047, and Moffitt Cancer Center, 12902 Magnolia Drive, Tampa, Florida 33612

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8007356

Reference50 articles.

1. Plant‐type ferredoxin‐NADP + reductases: a basal structural framework and a multiplicity of functions

2. Enzymic Mechanisms of Pyridine Nucleotide Reduction in Chloroplasts

3. NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon.

4. The seven-iron FdI from Azotobacter vinelandii regulates the expression of NADPH: ferredoxin reductase via an oxidative stress response

5. The oxidant-responsive diaphorase ofRhodobacter capsulatusis a ferredoxin (flavodoxin)-NADP(H) reductase

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