Aldehyde: ferredoxin oxidoreductase Pyrococcus furiosus

Mukund S, MWW Adams (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. J Biol Chem 266 14208-14216. 

Pyrimidinethione complexes, osmium, 37 296 Pyriminethionate, as bridging ligands in platinum dimers, 40 202-205 Pyrochlores, 17 108 Pyrococcus furiosus, 38 344-383 aldehyde ferredoxin oxidoreductase, 38 374-381... 

The aldehyde ferredoxin oxidoreductase from the hyperthermophile Pyrococcus furiosus was the first molybdopterin-dependent enzyme for which a three-dimensional structure became available.683,684 The tungstoenzyme resembles that of the related molybdo-enzyme (Fig. 16-31). A similar ferredoxin-dependent enzyme reduces glyceraldehyde-3-phosphate.685 Another member of the tungstoenzyme aldehyde oxidoreductase family is carboxylic acid reductase, an enzyme found in certain acetogenic clostridia. It is able to use reduced ferredoxin to convert unactivated carboxylic acids into aldehydes, even though E° for the acetaldehyde/acetate couple is -0.58 V.686... 

The crystal structure of aldehyde ferredoxin oxidoreductase (AOR) from the hyperthermophile Pyrococcus furiosus was the first of any molybdenum or tungsten enzyme (excepting nitrogenase) (42). The AOR was adopted as the parent name for the family of tungsten enzymes. The structure of formaldehyde ferredoxin oxidoreductase (FOR) has recently been solved (44). 

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