Role of specific residues in coenzyme binding, charge–transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase-Reference-Cited by-同舟云学术

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Role of specific residues in coenzyme binding, charge–transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase

Published:2010-09 Issue:9 Volume:1797 Page:1638-1646
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Peregrina José Ramón,Sánchez-Azqueta Ana,Herguedas Beatriz,Martínez-Júlvez Marta,Medina Milagros

Funder

Ministerio de Educación y Ciencia, Spain

CONSI+D

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference48 articles.

1. Open questions in ferredoxin-NADP+ reductase catalytic mechanism;Carrillo;Eur. J. Biochem.,2003

2. X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8Å resolution, and crystallographic studies of NADP+ binding at 2.25Å resolution;Serre;J. Mol. Biol.,1996

3. Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family;Karplus;Science,1991

4. Photosynthesis: Mechanisms and Effects;Carrillo,1998

5. The plant-type ferredoxin-NADP+ reductase/ferredoxin redox system as a possible drug target against apicomplexan human parasites;Seeber;Curr. Pharm. Des.,2005

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1. Nanomechanical Study of Enzyme: Coenzyme Complexes: Bipartite Sites in Plastidic Ferredoxin-NADP+ Reductase for the Interaction with NADP+;Antioxidants;2022-03-11

2. Adaptation of cyanobacterial photosynthesis to metal constraints;Expanding Horizon of Cyanobacterial Biology;2022

3. Kinetic and structural insight into a role of the re-face Tyr328 residue of the homodimer type ferredoxin-NADP+ oxidoreductase from Rhodopseudomonas palustris in the reaction with NADP+/NADPH;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2020-03

4. Metalloproteins in the Biology of Heterocysts;Life;2019-04-03

5. The catalytic mechanism of electron-bifurcating electron transfer flavoproteins (ETFs) involves an intermediary complex with NAD+;Journal of Biological Chemistry;2019-03

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