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Nitrite/Sulfite reductase ferredoxin-like half domain
Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidised anions for energy transduction [1]. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain. [1]. 7569952. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Crane BR, Siegel LM, Getzoff ED;. Science 1995;270:59-67. (from Pfam)
Nitrite and sulphite reductase 4Fe-4S domain
Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidised anions for energy transduction. [1]. 7569952. Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. Crane BR, Siegel LM, Getzoff ED;. Science 1995;270:59-67. [2]. 9315849. Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products. Crane BR, Siegel LM, Getzoff ED;. Biochemistry 1997;36:12120-12137. (from Pfam)
precorrin-3B synthase
An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively.
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