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J. Biol. Chem., Vol. 277, Issue 19, 17101-17107, May 10, 2002

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Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP⁺ Reductase with Residual NADP⁺ Binding Domain^*

Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda^§, Toshiharu Hase, and Yuji Goto^¶

From the Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan

Maize ferredoxin-NADP⁺ reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP⁺ binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP⁺ binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP⁺ binding domain but a disordered FAD binding domain.

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