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High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily.

Kean KM, Carpenter RA, Pandini V, Zanetti G, Hall AR, Faber R, Aliverti A, Karplus PA
FEBS J 284 3302-3319 (2017)
Related entries: 5vw2, 5vw4, 5vw5, 5vw6, 5vw7, 5vw8, 5vw9, 5vwa, 5vwb

Cited: 7 times
EuropePMC logo PMID: 28783258

Abstract

Ferredoxin: NADP+ reductase (FNR) is an FAD-containing enzyme best known for catalysing the transfer of electrons from ferredoxin (Fd) to NADP+ to make NADPH during photosynthesis. It is also the prototype for a broad enzyme superfamily, including the NADPH oxidases (NOXs) that all catalyse similar FAD-enabled electron transfers between NAD(P)H and one-electron carriers. Here, we define further mechanistic details of the NAD(P)H ⇌ FAD hydride-transfer step of the reaction based on spectroscopic studies and high-resolution (~ 1.5 Å) crystallographic views of the nicotinamide-flavin interaction in crystals of corn root FNR Tyr316Ser and Tyr316Ala variants soaked with either nicotinamide, NADP+ , or NADPH. The spectra obtained from FNR crystal complexes match those seen in solution and the complexes reveal active site packing interactions and patterns of covalent distortion of the FAD that imply significant active site compression that would favour catalysis. Furthermore, anisotropic B-factors show that the mobility of the C4 atom of the nicotinamide in the FNR:NADP+ complex has a directionality matching that expected for boat-like excursions of the nicotinamide ring thought to enhance hydride transfer. Arguments are made for the relevance of this binding mode to catalysis, and specific consideration is given to how the results extrapolate to provide insight to structure-function relations for the membrane-bound NOX enzymes for which little structural information has been available.

Articles - 5vw3 mentioned but not cited (1)

  1. High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily. Kean KM, Carpenter RA, Pandini V, Zanetti G, Hall AR, Faber R, Aliverti A, Karplus PA. FEBS J 284 3302-3319 (2017)


Reviews citing this publication (2)

  1. Transfer hydrogenation catalysis in cells. Banerjee S, Sadler PJ. RSC Chem Biol 2 12-29 (2021)
  2. Roles of Ferredoxin-NADP+ Oxidoreductase and Flavodoxin in NAD(P)H-Dependent Electron Transfer Systems. Iyanagi T. Antioxidants (Basel) 11 2143 (2022)

Articles citing this publication (4)

  1. Engineering stability in NADPH oxidases: A common strategy for enzyme production. Ceccon M, Millana Fananas E, Massari M, Mattevi A, Magnani F. Mol Membr Biol 34 67-76 (2017)
  2. CRISPR-gene-engineered CYBB knock-out PLB-985 cells, a useful model to study functional impact of X-linked chronic granulomatous disease mutations: application to the G412E X91+-CGD mutation. Beaumel S, Verbrugge L, Fieschi F, Stasia MJ. Clin Exp Immunol 212 156-165 (2023)
  3. Identifying structural and dynamic changes during the Biliverdin Reductase B catalytic cycle. Lee E, McLeod MJ, Redzic JS, Marcolin B, Thorne RE, Agarwal P, Eisenmesser EZ. Front Mol Biosci 10 1244587 (2023)
  4. Targeting ROS production through inhibition of NADPH oxidases. Reis J, Gorgulla C, Massari M, Marchese S, Valente S, Noce B, Basile L, Törner R, Cox H, Viennet T, Yang MH, Ronan MM, Rees MG, Roth JA, Capasso L, Nebbioso A, Altucci L, Mai A, Arthanari H, Mattevi A. Nat Chem Biol (2023)


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