Role of Arg100 and Arg264 from Anabaena PCC 7119 Ferredoxin−NADP+ Reductase for Optimal NADP+ Binding and Electron Transfer-Reference-Cited by-同舟云学术

Role of Arg100 and Arg264 from Anabaena PCC 7119 Ferredoxin−NADP+ Reductase for Optimal NADP+ Binding and Electron Transfer

Published:1998-12-01 Issue:51 Volume:37 Page:17680-17691
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Martínez-Júlvez Marta¹,Hermoso Juan¹,Hurley John K.¹,Mayoral Tomás¹,Sanz-Aparicio Julia¹,Tollin Gordon¹,Gómez-Moreno Carlos¹,Medina Milagros¹

Affiliation:

1. Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, 50009 Zaragoza, Spain, Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain, and Department of Biochemistry, University of Arizona, Tucson, Arizona 85721

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi981718i

Reference56 articles.

1. Studies on the one- and two-electron FAD-mediated reactions by ferrodoxin-NADP+ oxidoreductase from Anabaena

2. Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7 Å Resolution: Oxidized, Reduced and 2′-Phospho-5′-AMP Bound States

3. Atomic Structure of Ferredoxin-NADP + Reductase: Prototype for a Structurally Novel Flavoenzyme Family

4. X-ray Structure of the Ferredoxin:NADP+Reductase from the CyanobacteriumAnabaenaPCC 7119 at 1.8 Å Resolution, and Crystallographic Studies of NADP+Binding at 2.25 Å Resolution

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