Structure-function relations for ferredoxin reductase

@article{Karplus1994StructurefunctionRF,
  title={Structure-function relations for ferredoxin reductase},
  author={P. Andrew Karplus and Christopher M. Bruns},
  journal={Journal of Bioenergetics and Biomembranes},
  year={1994},
  volume={26},
  pages={89-99}
}
  • P. Karplus, C. M. Bruns
  • Published 1 February 1994
  • Chemistry, Biology
  • Journal of Bioenergetics and Biomembranes
Ferredoxin:NADP+ reductase is representative of a large family of flavoenzymes which catalyze the interchange of reducing equivalents between one-electron carriers and the two-electron-carrying nicotinamide dinucleotides. The structure of the enzyme from spinach is known at 1.7 Å resolution and this structure, together with results of chemical modification and site-directed mutagenesis studies, gives insights into features of the structure that are important for function. 
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90 Citations
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Structural Aspects of Plant Ferredoxin : NADP+ Oxidoreductases
TLDR
A structurally informed cycle for FNR catalysis in vivo is proposed and insight into its structure–function relations is summarized and combined to propose a structurallyinformed cycle.
Structure-function relationships in the ferredoxin/ferredoxin: NADP+ reductase system from Anabaena.
Ferredoxin and Ferredoxin-Dependent Enzymes
TLDR
This chapter describes the current state of the knowledge of the structure of ferredoxin and of these ferred toxin-dependent enzymes, of the biosynthesis of these proteins and of the mode of interaction between fer redoxin and its electron-accepting, reaction-partner proteins.
A productive NADP+ binding mode of ferredoxin–NADP + reductase revealed by protein engineering and crystallographic studies
TLDR
It is shown that nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain, and the structures of productive NADP+ and NADPH complexes are revealed.
Interaction of Ferredoxin–NADP+ Reductase with its Substrates: Optimal Interaction for Efficient Electron Transfer
TLDR
The present manuscript summarises the information so far reported for an efficient interaction between F NR and its substrates, compares such information with that revealed by other systems for which the FNR structure is a prototype, and discusses the implications of the processes of association in ET between FNR and its substrateates.
Probing the Function of the Invariant Glutamyl Residue 312 in Spinach Ferredoxin-NADP+ Reductase*
TLDR
Glu-312 does not fulfil the role of proton donor during catalysis, but it is required for proper binding of the nicotinamide ring of NADP(H), and its charge modulates the two one-electron redox potentials of the flavin to stabilize the semiquinone form.
Structural and functional diversity of ferredoxin-NADP(+) reductases.
Investigation of the diaphorase reaction of ferredoxin-NADP+ reductase by electrochemical methods
Open questions in ferredoxin-NADP+ reductase catalytic mechanism.
TLDR
Using the formalism of the Albery-Knowles theory, which identifies which parameter(s) have to be modified to make these reductases even more proficient under a variety of conditions, natural or artificial, a rationale to interpret FNR evolution in terms of catalytic efficiency is provided.
External loops at the ferredoxin-NADP(+) reductase protein-partner binding cavity contribute to substrates allocation.
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References

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Structure-function relationship in spinach ferredoxin-NADP+ reductase as studied by limited proteolysis.
Crystals of Anabaena PCC 7119 ferredoxin-NADP+ reductase.
Spirulina ferredoxin-NADP+ reductase. The complete amino acid sequence.
TLDR
An apparent homology of the amino(N)-terminal region was found between ferredoxin-NADP+ reductases from Spirulina and spinach and some sequence similarities in human erythrocyte glutathione reductase and p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, both of which are NADPH-dependent FAD enzymes.
On the reactivity of the sulfhydryl groups of ferredoxin nicotinamide adenine dinucleotide phosphate reductase.
Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family.
TLDR
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 reduct enzyme, NAD PH-sulfite reductases, NADH-cy tochrome b5 reductasing enzymes, and NADh-nitrate reduCTase.
FAD analogues as mechanistic and 'binding-domain' probes of spinach ferredoxin-NADP+ reductase.
The native flavin, FAD, of spinach ferredoxin--NADP+ reductase, has been replaced by a number of FAD analogues with modifications of the isoalloxazine ring system. The apoenzyme binds 8-mercapto-FAD…
The light-dependent modulation of photosynthetic electron transport
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TLDR
Stopped-flow experiments showed that the enzyme-FAD reduction rate was considerably decreased in the C272S mutant reductase, along with a much lower yield of the charge-transfer transient species, inferred from these data that the charge transfer is required for hydride transfer from the pyridine nucleotide to flavin to occur with a rate compatible with catalysis.
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].
TLDR
Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP(+)-reductase, many of which are related to plant ferredoxins.
Electron transfer by ferredoxin:NADP+ reductase. Rapid-reaction evidence for participation of a ternary complex.
TLDR
Premixing Fd with FNR was found to inhibit the reaction of the flavoprotein with NADP+ and with NADPH; thus, substrate binding may be ordered, NADP+, first, then Fd.
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