Photosynthetic pyridine nucleotide

Isolation of "Photosynthetic Pyridine Nucleotide Reductase (PPNR) from spinach chloroplasts... 

Crystallization of Clostridium pasteurianum ferredoxin demonstration of functional interchangeability of spinach photosynthetic pyridine nucleotide reductase and bacterial ferredoxin suggestion that both be classified as ferredoxins... 

In 1956, San Pietro and Lang (87) found that the soluble fraction from chloroplasts was necessary for the photoreduction of DPN when a small amount of chloroplasts was used. Two years later, San Pietro and Lang (88) reported the purification of a factor from the soluble fraction, which they described as an enzyme named photosynthetic pyridine nucleotide reductase (PPNR). In earlier experiments, the preferred acceptor was DPN (San Pietro and Lang (87) but with the partially purified enzyme the rate of DPN reduction was 70 percent that observed with TPN (San Pietro and Lang (88)). 

Apella, E., and A. San Pietro Physical properties of photosynthetic pyridine nucleotide reductase. Biochem. Biophys. Res. Commun. 6, 349—358 (1962). 

Photosynthetic pyridine nucleotide reductase. IV. Further studies on the chemical properties of the protein. In Photosynthesis Mechanisms in Green Plants, Publ. 1145, Nat. Acad. Sci.-Nat. Res. Council (U. S.), pp. 252—26 (1963). 

Photosynthetic pyridine nucleotide reductase. I. Partial purification and... 

Shapiro, D. M. The purification and properties of photosynthetic pyridine nucleotide reductase from Euglena gracilis. Doctoral Thesis, Johns Hopkins University, Baltimore, Md. Quoted by San Pietro and Black (1965) (1961). 

All of these properties are strikingly similar to those of spinach ferredoxin, which serves as an oxidation-reduction intermediate in photosynthetic pyridine nucleotide reduction. Thus, it is assumed that the fundamental chemical nature of the iron environment in both of these two iron proteins is identical. 

An important difference between animal and plant electron transferring proteins is the non-exchangeability in their physiological functions adrenodoxin is inactive for photosynthetic pyridine nucleotide reduction and spinach ferredoxin does not function in adrenal steroid hydroxy-... 

Spinach ferredoxin photosynthetic pyridine nucleotide reduction (19, 63) inactive... 

San Pietro A, Lang HM Photosynthetic pyridine nucleotide reductase. 1. Partial purification and properties of the enzyme from spinach. J Biol Chem 1958, 231(l) 211-229. 

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