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Cited by 536Enzyme Structure and FunctionProtein Structure and DynamicsMetalloenzymes and iron-sulfur proteins

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

Karplus, P. Andrew, Daniels, Mark J., Herriott, Jon R.·1991·Science
DOI 10.1126/science.1986412
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Abstract

The three-dimensional structure of spinach ferredoxin- NADP + reductase (NADP + nicotinamide adenine dinucleotide phosphate) has been determined by x-ray diffraction at 2.6 angstroms (Å) resolution and initially refined to an R factor of 0.226 at 2.2 Å resolution. The model includes the flavin-adenine dinucleotide (FAD) prosthetic group and the protein chain from residue 19 through the carboxyl terminus at residue 314 and is composed of two domains. The FAD binding domain (residues 19 to 161) has an antiparallel β barrel core and a single α helix for binding the pyrophosphate of FAD. The NADP binding domain (residues 162 to 314) has a central five-strand parallel β sheet and six surrounding helices. Binding of the competitive inhibitor 2′-phospho-AMP (AMP, adenosine monophosphate) places the NADP binding site at the carboxyl-terminal edge of the sheet in a manner similar to the nucleotide binding of the dehydrogenase family. The structures reveal the key residues that function in cofactor binding and the catalytic center. With these key residues as a guide, conclusive evidence is presented that the ferredoxin reductase structure is a prototype for the nicotinamide dinucleotide and FAD binding domains of the enzymes NADPH-cytochrome P450 reductase, NADPH-sulfite reductase, NADH-cytochrome b 5 reductase, and NADH-nitrate reductase. Thus this structure provides a structural framework for the NADH- or NADPH-dependent flavoenzyme parts of five distinct enzymes involved in photosynthesis, in the assimilation of inorganic nitrogen and sulfur, in fatty-acid oxidation, in the reduction of methemoglobin, and in the metabolism of many pesticides, drugs, and carcinogens.

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  • NOX core subunits 1-4 are structurally similar with an N-terminal membrane domain and a C-terminal flavoprotein dehydrogenase domain with high sequence homology to the ferredoxin/NADP reductase family.

    “NOX core subunits 1–4 are structurally similar with a N-terminal, membrane domain and a C-terminal flavoprotein, dehydrogenase domain with high sequence homology to the ferredoxin/NADP reductase family (490).”

    From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [490]

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Authors
Karplus, P. A., Daniels, M. J., & Herriott, J. R.
Affiliations
  • Cornell University (US)
  • University of Washington (US)
ORCID
Karplus, P. Andrew
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1991-01-04
Volume
251
Issue
4989
Pages
60-66
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1986412
OpenAlex
W2006369456
Cited by
536
References
70
Citations by year
2025: 5 · 2024: 6 · 2023: 9 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 6 · 2018: 3 · 2017: 8 · 2016: 6 · 2015: 4 · 2014: 6 · 2013: 10 · 2012: 10
FWCI
46.15
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
ferredoxin-NADP+ reductase, flavoenzyme, flavin adenine dinucleotide, protein structure, FAD-binding domain, NADPH-cytochrome P450 reductase, NADH-cytochrome b5 reductase, NADH-nitrate reductase, structural homology, photosynthesis, nitrogen assimilation, sulfur assimilation, methemoglobin reduction, cofactor binding, catalytic site
MeSH terms
Adenosine Diphosphate, Amino Acid Sequence, Binding Sites, Crystallization, Flavin-Adenine Dinucleotide, Ferredoxin-NADP Reductase, Ferredoxins, Hydrogen Bonding, Molecular Sequence Data, NADP, Nucleotides, Plants, Protein Conformation, Sequence Homology, Nucleic Acid, X-Ray Diffraction, Molecular Structure

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