k 2Fe2S ferredoxin core, molecular model 2Fe2S ferredoxin core, molecular model. Ferredoxin electron transfer proteins are widespread among organisms and versatile in their redox chemistry. The active sites of these enzymes are clusters of iron orange and sulphur yellow atoms, usually either 2Fe2S or 4Fe4S. In either case, the cluster is bonded to four cysteine residues resulting in FeS4 tetrahedra. Shown here is the 2Fe2S cluster structure, paired with putidaredoxin, a small bacterial ferredoxin., by 39 Stock Photo - Afloimages
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2Fe 2S ferredoxin core, molecular model 2Fe 2S ferredoxin core, molecular model. Ferredoxin electron transfer proteins are widespread among organisms and versatile in their redox chemistry. The active sites of these enzymes are clusters of iron  orange  and sulphur  yellow  atoms, usually either  2Fe 2S  or  4Fe 4S . In either case, the cluster is bonded to four cysteine residues resulting in FeS4 tetrahedra. Shown here is the  2Fe 2S  cluster structure, paired with putidaredoxin, a small bacterial ferredoxin., by 39
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2Fe-2S ferredoxin core, molecular model

2Fe-2S ferredoxin core, molecular model. Ferredoxin electron transfer proteins are widespread among organisms and versatile in their redox chemistry. The active sites of these enzymes are clusters of iron (orange) and sulphur (yellow) atoms, usually either [2Fe-2S] or [4Fe-4S]. In either case, the cluster is bonded to four cysteine residues resulting in FeS4 tetrahedra. Shown here is the [2Fe-2S] cluster structure, paired with putidaredoxin, a small bacterial ferredoxin., by 39

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