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Structure of ferredoxin-NADP+ oxidoreductase and the location of the NADP binding site

1981; Elsevier BV; Volume: 145; Issue: 2 Linguagem: Inglês

10.1016/0022-2836(81)90214-x

1089-8638

S. Sheriff, Jon R. Herriott,

Metal-Catalyzed Oxygenation Mechanisms

Ferredoxin-NADP+ oxidoreductase is the enzyme responsible for catalyzing the production of NADPH during photosynthesis. The structure of “ferredoxin reductase” has been elucidated at 3.7 Å resolution by the method of multiple isomorphous replacement with anomalous scattering. The molecule consists of two structural domains, as anticipated for an enzyme that binds two nucleotides, FAD and NADP. The NADP binding site has been located by means of a difference Fourier map. This coenzyme binds at the carboxyl end of the first strand of a four-strand parallel pleated sheet near the amino end of several adjacent helices. The binding appears similar to that of nicotinamide nucleotides in other proteins. We report here an overall description of the shape of the molecule, a preliminary interpretation of the folding of the polypeptide chain in the NADP binding domain and the location of the NADP binding site.