The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
Molybdopterin cofactor, shown in the dithiol protonation state.
The redox reactions of nicotinamide adenine dinucleotide.
AOR mechanism at the active site.

The active site of the AOR family feature an oxo-tungsten center bound to a pair of molybdopterin cofactors (which does not contain molybdenum) and an 4Fe-4S cluster.

- Aldehyde ferredoxin oxidoreductase

Other organisms require additional metals as enzyme cofactors, such as vanadium in the nitrogenase of the nitrogen-fixing bacteria of the genus Azotobacter, tungsten in the aldehyde ferredoxin oxidoreductase of the thermophilic archaean Pyrococcus furiosus, and even cadmium in the carbonic anhydrase from the marine diatom Thalassiosira weissflogii.

- Cofactor (biochemistry)
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.

0 related topics with Alpha

Overall