k 4Fe4S ferredoxin core, molecular model 4Fe4S 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 4Fe4S cluster structure, paired with an example of a bacterial ferredoxin that has two copies of the 4Fe4S cluster., by 39 Stock Photo - Afloimages
Sign up
Login
All images
4Fe 4S ferredoxin core, molecular model 4Fe 4S 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  4Fe 4S  cluster structure, paired with an example of a bacterial ferredoxin that has two copies of the  4Fe 4S  cluster., by 39
RM

4Fe-4S ferredoxin core, molecular model

4Fe-4S 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 [4Fe-4S] cluster structure, paired with an example of a bacterial ferredoxin that has two copies of the [4Fe-4S] cluster., by 39

Details

ID
187206891

Collection

License type
Rights Managed

Photographer



Sign in
Member access
Login not found.