High-resolution studies of hydride transfer in the ferredoxin:NADP [electronic resource]
Producer: 20171020Description: 3302-3319 p. digitalISSN:- 1742-4658
- Amino Acid Sequence
- Binding Sites
- Biocatalysis
- Catalytic Domain
- Cloning, Molecular
- Crystallography, X-Ray
- Escherichia coli -- genetics
- Ferredoxin-NADP Reductase -- chemistry
- Flavin-Adenine Dinucleotide -- chemistry
- Gene Expression
- Humans
- Kinetics
- Models, Molecular
- NAD -- chemistry
- NADP -- chemistry
- NADPH Oxidases -- chemistry
- Plant Proteins -- chemistry
- Plant Roots -- chemistry
- Protein Binding
- Protein Interaction Domains and Motifs
- Protein Structure, Secondary
- Recombinant Proteins -- chemistry
- Sequence Alignment
- Sequence Homology, Amino Acid
- Substrate Specificity
- Zea mays -- chemistry
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Publication Type: Journal Article
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