BACTERIAL FERREDOXIN

The Structure of a Bacterial Ferredoxin

The structure of the bacterial ferredoxin from Peptococcus aerogenes (54 amino acids) has been determined at 2.8 A resolution. The molecule is a prolate ellipsoid with approximate dimension of 22 x 27 A. The iron and sulfur atoms are in two complexes 12 A apart with 4 iron, 4 inorganic sulfur, and 4 cysteine sulfur atoms in each. Cys 8, 11, 14, and 45 are coordinated to iron atoms in one comple...

Structure of the bacterial plant-ferredoxin receptor FusA

Iron is a limiting nutrient in bacterial infection putting it at the centre of an evolutionary arms race between host and pathogen. Gram-negative bacteria utilize TonB-dependent outer membrane receptors to obtain iron during infection. These receptors acquire iron either in concert with soluble iron-scavenging siderophores or through direct interaction and extraction from host proteins. Charact...

Ferredoxin as a Reductant in Pyruvate Synthesis by a Bacterial Extract.

Enhanced plant tolerance to iron starvation by functional substitution of chloroplast ferredoxin with a bacterial flavodoxin.

Iron limitation affects one-third of the cultivable land on Earth and represents a major concern for agriculture. It causes decline of many photosynthetic components, including the Fe-S protein ferredoxin (Fd), involved in essential oxidoreductive pathways of chloroplasts. In cyanobacteria and some algae, Fd down-regulation under Fe deficit is compensated by induction of an isofunctional electr...

Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution.

The reduction of ferredoxin-thioredoxin reductase (FTR) by plant-type ferredoxin plays an important role in redox regulation in plants and cyanobacteria. Nuclear magnetic resonance (NMR) was used to map the binding sites on Synechocystis ferredoxin for FTR. A gallium-substituted structural analog of this [2Fe-2S] ferredoxin was obtained by reconstituting the apoprotein in a refolding buffer con...